Thomas A. Steitz

Communicated by J.N. Reeve (2009)

Daqi Tu, Æ Gregor, Blaha Æ Peter, B. Moore, Thomas A. Steitz, P. B. Moore, ...

Gene replacement in Haloarcula marismortui: construction of a strain

The Structures of Antibiotics Bound to the E Site Region of the 50 S Ribosomal Subunit of Haloarcula (2009)

Marismortui -deoxytedanolide, Susan J. Schroeder, Gregor Blaha, Julian Tirado-rives, Thomas A. Steitz, Peter B. Moore, ...

Crystal structures of the 50 S ribosomal subunit from Haloarcula marismortui complexed with two antibiotics have identified new sites at which antibiotics interact with the ribosome and inhibit...

Structures of Five Antibiotics Bound at the Peptidyl (2008)

Transferase Center Of, Jeffrey L. Hansen, Peter B. Moore, Thomas A. Steitz, Howard Hughes Medical

ding author Introduction Antibiotics are compounds of natural or synthetic origin that selectively kill or inhibit the growth of microorganisms, and many of them are sufficiently specific to be...

Peptidyl-CCA deacylation on the ribosome promoted by induced fit and the O3'-hydroxyl group of A76 of the unacylated A-site tRNA (2008)

Simonovic, Miljan, Steitz, Thomas A.

The last step in ribosome-catalyzed protein synthesis is the hydrolytic release of the newly formed polypeptide from the P-site bound tRNA. Hydrolysis of the ester link of the peptidyl-tRNA is...

Biophysics and Biochemistry (2007)

Fang Li, Jimin Wang, Thomas A. Steitz

The tRNA CCA-adding enzyme is an RNA polymerase that catalyzes the untemplated synthesis and repair of the 3 0 terminal CCA sequence of transfer RNA molecules. The major puzzle presented

the ribosome is a ribozyme (2007)

Thomas A. Steitz, Peter B. Moore

RNA, the first macromolecular catalyst:

The crystal structure of the Thermus aquaticus DnaB helicase monomer (2007)

Bailey, Scott, Eliason, William K., Steitz, Thomas A.

The ring-shaped hexameric DnaB helicase unwinds duplex DNA at the replication fork of eubacteria. We have solved the crystal structure of the full-length Thermus aquaticus DnaB monomer, or possibly...

The contribution of metal ions to the structural stability of the large ribosomal subunit (2004)

KLEIN, DANIEL J., MOORE, PETER B., STEITZ, THOMAS A.

Both monovalent cations and magnesium ions are well known to be essential for the folding and stability of large RNA molecules that form complex and compact structures. In the atomic structure of the...

After the ribosome structures: How does peptidyl transferase work? (2003)

MOORE, PETER B., STEITZ, THOMAS A.

Atomic resolution crystal structures of the large subunit published since the middle of August 2000 prove that the peptidyl transferase center of the ribosome, which is the site of peptide-bond...

Structures of deacylated tRNA mimics bound to the E site of the large ribosomal subunit (2003)

SCHMEING, T. MARTIN, MOORE, PETER B., STEITZ, THOMAS A.

During translation, tRNAs cycle through three binding sites on the ribosome: the A, the P, and the E sites. We have determined the structures of complexes between the Haloarcula marismortui large...

Protein Engineering vol.15 no.6 pp.485--492, 2002 (2002)

Rational Design Of, Thomas A. Steitz

t solubilization in aqueous media. We have discussed the feasibility of applying the `solubilization strategy' outlined here to membrane proteins. Keywords: bacteriorhodopsin/folding/membrane...

Assembly, purification and crystallization of an active HIV-1 reverse transcriptase initiation complex (2002)

Pata, Janice D., King, Bradford R., Steitz, Thomas A.

Human immunodeficiency virus type 1 (HIV‐1) reverse transcriptase (RT) initiates DNA synthesis from the 3′ end of human tRNALys3. We have used cis‐acting hammerhead ribozymes to produce...

Conversion of phospholamban into a soluble pentameric helical bundle. Biochemistry 40: 6636–6645 (2001)

Huiming Li, Melanie J. Cocco, Thomas A. Steitz, Donald M. Engelman

ABSTRACT: Although membrane proteins and soluble proteins may achieve their final folded states through different pathways, it has been suggested that the packing inside a membrane protein could...

The Complete Atomic Structure of the Large Ribosomal Subunit at 2.4 Å Resolution (2000)

Nenad Ban, Poul Nissen, Jeffrey Hansen, Peter B. Moore, Thomas A. Steitz

ation, and termination phases of protein synthesis. Because the structures of several DNA and RNA polymerases have been determined at atomic resolution, the mechanisms of DNA and RNA synthesis are...

Comparison of the Crystal and Solution Structures of Two RNA Oligonucleotides (1999)

Rna Oligonucleotides, Jason P. Rife, Sarah C. Stallings, Carl C. Correll, Anne Dallas, Thomas A. Steitz, ...

Until recently, there were no examples of RNAs whose structures had been determined by both NMR and x-ray crystallography, and thus there was no experimental basis for assessing the accuracy of RNA...

Ribosomal protein L7/L12 has a helix-turn-helix motif similar to that found in DNA-binding regulatory proteins (1989)

Rice, Phoebe A., Steitz, Thomas A.

Inspection of the structure of the C-terminal domain of ribosomal protein L7/L12 (1) reveals a helix-turn-helix motif similar to the one found in many DNA-binding regulatory proteins (2–5). The 19...

A model for the non-specific binding of catabolite gene activator protein to DNA (1984)

Weber, Irene T., Steitz, Thomas A.

The binding of E. coli catabollte gene activator protein (CAP) to non-specific sequences of DNA has been modelled as an electrostatic interaction between four basic side chains of the CAP dimer and...

Structure of Escherichia coli ribosomal protein L25 complexed with a 5S rRNA fragment at 1.8-Å resolution

Lu, Min, Steitz, Thomas A.

The crystal structure of Escherichia coli ribosomal protein L25 bound to an 18-base pair portion of 5S ribosomal RNA, which contains “loop E,” has been determined at 1.8-Å resolution. The...

A 1.3-Å resolution crystal structure of the HIV-1 trans-activation response region RNA stem reveals a metal ion-dependent bulge conformation

Ippolito, Joseph A., Steitz, Thomas A.

The crystal structure of an HIV-1 trans-activation response region (TAR) RNA fragment containing the binding site for the trans-activation protein Tat has been determined to 1.3-Å resolution. In...

Crystal structure of the ribosomal RNA domain essential for binding elongation factors

Correll, Carl C., Munishkin, Alexander, Chan, Yuen-Ling, Ren, Zhong, Wool, Ira G., Steitz, Thomas A.

The structure of a 29-nucleotide RNA containing the sarcin/ricin loop (SRL) of rat 28 S rRNA has been determined at 2.1 Å resolution. Recognition of the SRL by elongation factors and by the...

RNA tertiary interactions in the large ribosomal subunit: The A-minor motif

Nissen, Poul, Ippolito, Joseph A., Ban, Nenad, Moore, Peter B., Steitz, Thomas A.

Analysis of the 2.4-Å resolution crystal structure of the large ribosomal subunit from Haloarcula marismortui reveals the existence of an abundant and ubiquitous structural motif that stabilizes...

Structural insights into peptide bond formation

Hansen, Jeffrey L., Schmeing, T. Martin, Moore, Peter B., Steitz, Thomas A.

The large ribosomal subunit catalyzes peptide bond formation and will do so by using small aminoacyl- and peptidyl-RNA fragments of tRNA. We have refined at 3-Å resolution the structures of both A...

Assembly, purification and crystallization of an active HIV-1 reverse transcriptase initiation complex

Pata, Janice D., King, Bradford R., Steitz, Thomas A.

Human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) initiates DNA synthesis from the 3′ end of human tRNALys3. We have used cis-acting hammerhead ribozymes to produce...

The structural basis of cysteine aminoacylation of tRNAPro by prolyl-tRNA synthetases

Kamtekar, Satwik, Kennedy, W. Dexter, Wang, Jimin, Stathopoulos, Constantinos, Söll, Dieter, Steitz, Thomas A.

Cysteinyl-tRNA synthetase is an essential enzyme required for protein synthesis. Genes encoding this protein have not been identified in Methanocaldococcus jannaschii, Methanothermobacter...

The lac Repressor Protein: Molecular Shape, Subunit Structure, and Proposed Model for Operator Interaction Based on Structural Studies of Microcrystals

Steitz, Thomas A., Richmond, Timothy J., Wise, David, Engelman, Donald

Electron microscopic and powder x-ray diffraction studies of small crystals of the lac repressor protein provide evidence on its molecular shape and subunit structure which in turn suggests a...

Structure of HIV-1 reverse transcriptase bound to an inhibitor active against mutant reverse transcriptases resistant to other nonnucleoside inhibitors

Pata, Janice D., Stirtan, William G., Goldstein, Steven W., Steitz, Thomas A.

We have determined the crystal structure of the HIV type 1 reverse transcriptase complexed with CP-94,707, a new nonnucleoside reverse transcriptase inhibitor (NNRTI), to 2.8-Å resolution. In...

A specific subdomain in φ29 DNA polymerase confers both processivity and strand-displacement capacity

Rodríguez, Irene, Lázaro, José M., Blanco, Luis, Kamtekar, Satwik, Berman, Andrea J., Wang, Jimin, ...

Recent crystallographic studies of φ29 DNA polymerase have provided structural insights into its strand displacement and processivity. A specific insertion named terminal protein region 2 (TPR2),...

Structures of deacylated tRNA mimics bound to the E site of the large ribosomal subunit

SCHMEING, T. MARTIN, MOORE, PETER B., STEITZ, THOMAS A.

During translation, tRNAs cycle through three binding sites on the ribosome: the A, the P, and the E sites. We have determined the structures of complexes between the Haloarcula marismortui large...

After the ribosome structures: How does peptidyl transferase work?

MOORE, PETER B., STEITZ, THOMAS A.

Atomic resolution crystal structures of the large subunit published since the middle of August 2000 prove that the peptidyl transferase center of the ribosome, which is the site of peptide-bond...

The contribution of metal ions to the structural stability of the large ribosomal subunit

KLEIN, DANIEL J., MOORE, PETER B., STEITZ, THOMAS A.

Both monovalent cations and magnesium ions are well known to be essential for the folding and stability of large RNA molecules that form complex and compact structures. In the atomic structure of the...

Structure of Escherichia coli ribosomal protein L25 complexed with a 5S rRNA fragment at 1.8-Å resolution

Lu, Min, Steitz, Thomas A.

The crystal structure of Escherichia coli ribosomal protein L25 bound to an 18-base pair portion of 5S ribosomal RNA, which contains “loop E,” has been determined at 1.8-Å resolution. The...

A 1.3-Å resolution crystal structure of the HIV-1 trans-activation response region RNA stem reveals a metal ion-dependent bulge conformation

Ippolito, Joseph A., Steitz, Thomas A.

The crystal structure of an HIV-1 trans-activation response region (TAR) RNA fragment containing the binding site for the trans-activation protein Tat has been determined to 1.3-Å resolution. In...

Crystal structure of the ribosomal RNA domain essential for binding elongation factors

Correll, Carl C., Munishkin, Alexander, Chan, Yuen-Ling, Ren, Zhong, Wool, Ira G., Steitz, Thomas A.

The structure of a 29-nucleotide RNA containing the sarcin/ricin loop (SRL) of rat 28 S rRNA has been determined at 2.1 Å resolution. Recognition of the SRL by elongation factors and by the...

RNA tertiary interactions in the large ribosomal subunit: The A-minor motif

Nissen, Poul, Ippolito, Joseph A., Ban, Nenad, Moore, Peter B., Steitz, Thomas A.

Analysis of the 2.4-Å resolution crystal structure of the large ribosomal subunit from Haloarcula marismortui reveals the existence of an abundant and ubiquitous structural motif that stabilizes...

Structural insights into peptide bond formation

Hansen, Jeffrey L., Schmeing, T. Martin, Moore, Peter B., Steitz, Thomas A.

The large ribosomal subunit catalyzes peptide bond formation and will do so by using small aminoacyl- and peptidyl-RNA fragments of tRNA. We have refined at 3-Å resolution the structures of both A...

Assembly, purification and crystallization of an active HIV-1 reverse transcriptase initiation complex

Pata, Janice D., King, Bradford R., Steitz, Thomas A.

Human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) initiates DNA synthesis from the 3′ end of human tRNALys3. We have used cis-acting hammerhead ribozymes to produce...

The structural basis of cysteine aminoacylation of tRNAPro by prolyl-tRNA synthetases

Kamtekar, Satwik, Kennedy, W. Dexter, Wang, Jimin, Stathopoulos, Constantinos, Söll, Dieter, Steitz, Thomas A.

Cysteinyl-tRNA synthetase is an essential enzyme required for protein synthesis. Genes encoding this protein have not been identified in Methanocaldococcus jannaschii, Methanothermobacter...

The lac Repressor Protein: Molecular Shape, Subunit Structure, and Proposed Model for Operator Interaction Based on Structural Studies of Microcrystals

Steitz, Thomas A., Richmond, Timothy J., Wise, David, Engelman, Donald

Electron microscopic and powder x-ray diffraction studies of small crystals of the lac repressor protein provide evidence on its molecular shape and subunit structure which in turn suggests a...

Structure of HIV-1 reverse transcriptase bound to an inhibitor active against mutant reverse transcriptases resistant to other nonnucleoside inhibitors

Pata, Janice D., Stirtan, William G., Goldstein, Steven W., Steitz, Thomas A.

We have determined the crystal structure of the HIV type 1 reverse transcriptase complexed with CP-94,707, a new nonnucleoside reverse transcriptase inhibitor (NNRTI), to 2.8-Å resolution. In...

A specific subdomain in φ29 DNA polymerase confers both processivity and strand-displacement capacity

Rodríguez, Irene, Lázaro, José M., Blanco, Luis, Kamtekar, Satwik, Berman, Andrea J., Wang, Jimin, ...

Recent crystallographic studies of φ29 DNA polymerase have provided structural insights into its strand displacement and processivity. A specific insertion named terminal protein region 2 (TPR2),...

Structures of deacylated tRNA mimics bound to the E site of the large ribosomal subunit

SCHMEING, T. MARTIN, MOORE, PETER B., STEITZ, THOMAS A.

During translation, tRNAs cycle through three binding sites on the ribosome: the A, the P, and the E sites. We have determined the structures of complexes between the Haloarcula marismortui large...

After the ribosome structures: How does peptidyl transferase work?

MOORE, PETER B., STEITZ, THOMAS A.

Atomic resolution crystal structures of the large subunit published since the middle of August 2000 prove that the peptidyl transferase center of the ribosome, which is the site of peptide-bond...

The contribution of metal ions to the structural stability of the large ribosomal subunit

KLEIN, DANIEL J., MOORE, PETER B., STEITZ, THOMAS A.

Both monovalent cations and magnesium ions are well known to be essential for the folding and stability of large RNA molecules that form complex and compact structures. In the atomic structure of the...

Implications of structures of synaptic tetramers of γδ resolvase for the mechanism of recombination

Kamtekar, Satwik, Ho, Roger S., Cocco, Melanie J., Li, Weikai, Boocock, Martin R., ...

The structures of two mutants of the site-specific recombinase, γδ resolvase, that form activated tetramers have been determined. One, at 3.5-Å resolution, forms a synaptic intermediate of...

Accuracy, lesion bypass, strand displacement and translocation by DNA polymerases.

Steitz, Thomas A, Yin, Y Whitney

The structures of DNA polymerases from different families show common features and significant differences that shed light on the ability of these enzymes to accurately copy DNA and translocate. The...

The φ29 DNA polymerase:protein-primer structure suggests a model for the initiation to elongation transition

Kamtekar, Satwik, Berman, Andrea J, Wang, Jimin, Lázaro, José M, De Vega, Miguel, Blanco, Luis, ...

The absolute requirement for primers in the initiation of DNA synthesis poses a problem for replicating the ends of linear chromosomes. The DNA polymerase of bacteriophage φ29 solves this problem by...

Visualizing polynucleotide polymerase machines at work

Steitz, Thomas A

The structures of T7 RNA polymerase (T7 RNAP) captured in the initiation and elongation phases of transcription, that of φ29 DNA polymerase bound to a primer protein and those of the multisubunit...

Toward understanding phosphoseryl-tRNACys formation: The crystal structure of Methanococcus maripaludis phosphoseryl-tRNA synthetase

Kamtekar, Satwik, Hohn, Michael J., Park, Hee-Sung, Schnitzbauer, Michael, Sauerwald, Anselm, Söll, Dieter, ...

A number of archaeal organisms generate Cys-tRNACys in a two-step pathway, first charging phosphoserine (Sep) onto tRNACys and subsequently converting it to Cys-tRNACys. We have determined, at...

The crystal structure of the Thermus aquaticus DnaB helicase monomer

Bailey, Scott, Eliason, William K., Steitz, Thomas A.

The ring-shaped hexameric DnaB helicase unwinds duplex DNA at the replication fork of eubacteria. We have solved the crystal structure of the full-length Thermus aquaticus DnaB monomer, or possibly...

Structure of pyrrolysyl-tRNA synthetase, an archaeal enzyme for genetic code innovation

Kavran, Jennifer M., Gundllapalli, Sarath, O'Donoghue, Patrick, Englert, Markus, Söll, Dieter, Steitz, Thomas A.

Pyrrolysine (Pyl), the 22nd natural amino acid and genetically encoded by UAG, becomes attached to its cognate tRNA by pyrrolysyl-tRNA synthetase (PylRS). We have determined three crystal structures...

Structures of phi29 DNA polymerase complexed with substrate: the mechanism of translocation in B-family polymerases

Berman, Andrea J, Kamtekar, Satwik, Goodman, Jessica L, Lázaro, José M, De Vega, Miguel, Blanco, Luis, ...

Replicative DNA polymerases (DNAPs) move along template DNA in a processive manner. The structural basis of the mechanism of translocation has been better studied in the A-family of polymerases than...

Cross-crystal averaging reveals that the structure of the peptidyl-transferase center is the same in the 70S ribosome and the 50S subunit

Simonović, Miljan, Steitz, Thomas A.

Recently, two crystal structures of the Thermus thermophilus 70S ribosome in the same functional state were determined at 2.8 and 3.7 Å resolution but were different throughout. The most...

The structure of LepA, the ribosomal back translocase

Evans, Robin N., Blaha, Gregor, Bailey, Scott, Steitz, Thomas A.

LepA is a highly conserved elongation factor that promotes the back translocation of tRNAs on the ribosome during the elongation cycle. We have determined the crystal structure of LepA from...

Peptidyl-CCA deacylation on the ribosome promoted by induced fit and the O3′-hydroxyl group of A76 of the unacylated A-site tRNA

Simonović, Miljan, Steitz, Thomas A.

The last step in ribosome-catalyzed protein synthesis is the hydrolytic release of the newly formed polypeptide from the P-site bound tRNA. Hydrolysis of the ester link of the peptidyl-tRNA is...

Structure of apo-CAP reveals that large conformational changes are necessary for DNA binding

Sharma, Hitesh, Yu, Shaoning, Kong, Jilie, Wang, Jimin, Steitz, Thomas A.

The binding of cAMP to the Escherichia coli catabolite gene activator protein (CAP) produces a conformational change that enables it to bind specific DNA sequences and regulate transcription, which...