Christian R. H. Raetz

LMSD: LIPID MAPS structure database (2007)

Sud, Manish, Fahy, Eoin, Cotter, Dawn, Brown, Alex, Dennis, Edward A., Glass, Christopher K., ...

The LIPID MAPS Structure Database (LMSD) is a relational database encompassing structures and annotations of biologically relevant lipids. Structures of lipids in the database come from four sources:...

Bordetella pertussis waaA Encodes a Monofunctional 2-Keto-3-Deoxy-d-manno-Octulosonic Acid Transferase That Can Complement an Escherichia coli waaA Mutation

Isobe, Tomoko, White, Kimberley A., Allen, Andrew G., Peacock, Michael, Raetz, Christian R. H., Maskell, Duncan J.

Bordetella pertussis lipopolysaccharide (LPS) contains a single 2-keto-3-deoxy-d-manno-octulosonic acid (Kdo) residue, whereas LPS from Escherichia coli contains at least two. Here we report that B....

Expression Cloning of a Pseudomonas Gene Encoding a Hydroxydecanoyl-Acyl Carrier Protein-Dependent UDP-GlcNAc Acyltransferase

Dotson, Garry D., Kaltashov, Igor A., Cotter, Robert J., Raetz, Christian R. H.

UDP-N-acetylglucosamine-3-O-acyltransferase (UDP-GlcNAc acyltransferase) catalyzes the first step of lipid A biosynthesis (M. S. Anderson and C. R. H. Raetz, J. Biol. Chem. 262:5159–5169, 1987). We...

Solution structure and dynamics of the outer membrane enzyme PagP by NMR

Hwang, Peter M., Choy, Wing-Yiu, Lo, Eileen I., Chen, Lu, Forman-Kay, Julie D., Raetz, Christian R. H., ...

The bacterial outer membrane enzyme PagP transfers a palmitate chain from a phospholipid to lipid A. In a number of pathogenic Gram-negative bacteria, PagP confers resistance to certain cationic...

Cardiolipin Accumulation in the Inner and Outer Membranes of Escherichia coli Mutants Defective in Phosphatidylserine Synthetase

Raetz, Christian R. H., Kantor, Gina D., Nishijima, Masahiro, Newman, Karl F.

Mutants of Escherichia coli defective in phosphatidylserine synthetase (pss) make less phosphatidylethanolamine than normal cells, and they are temperature sensitive for growth. We have isolated a...

Diglyceride Kinase Mutants of Escherichia coli: Inner Membrane Association of 1,2-Diglyceride and Its Relation to Synthesis of Membrane-Derived Oligosaccharides

Raetz, Christian R. H., Newman, Karl F.

Mutants of Escherichia coli defective in diglyceride kinase contain 10 to 20 times more sn-1,2-diglyceride than normal cells. This material constitutes about 8% of the total lipid in such strains. We...

Transfer of palmitate from phospholipids to lipid A in outer membranes of Gram-negative bacteria

Bishop, Russell E., Gibbons, Henry S., Guina, Tina, Trent, M.Stephen, Miller, Samuel I., Raetz, Christian R.H.

Regulated covalent modifications of lipid A are implicated in virulence of pathogenic Gram-negative bacteria. The Salmonella typhimurium PhoP/PhoQ-activated gene pagP is required both for...

Molecular Validation of LpxC as an Antibacterial Drug Target in Pseudomonas aeruginosa

Mdluli, Khisimuzi E., Witte, Pamela R., Kline, Toni, Barb, Adam W., Erwin, Alice L., Mansfield, Bryce E., ...

LpxC [UDP-3-O-(R-3-hydroxymyristoyl)-GlcNAc deacetylase] is a metalloamidase that catalyzes the first committed step in the biosynthesis of the lipid A component of lipopolysaccharide. A previous...

Bordetella pertussis waaA Encodes a Monofunctional 2-Keto-3-Deoxy-d-manno-Octulosonic Acid Transferase That Can Complement an Escherichia coli waaA Mutation

Isobe, Tomoko, White, Kimberley A., Allen, Andrew G., Peacock, Michael, Raetz, Christian R. H., Maskell, Duncan J.

Bordetella pertussis lipopolysaccharide (LPS) contains a single 2-keto-3-deoxy-d-manno-octulosonic acid (Kdo) residue, whereas LPS from Escherichia coli contains at least two. Here we report that B....

Expression Cloning of a Pseudomonas Gene Encoding a Hydroxydecanoyl-Acyl Carrier Protein-Dependent UDP-GlcNAc Acyltransferase

Dotson, Garry D., Kaltashov, Igor A., Cotter, Robert J., Raetz, Christian R. H.

UDP-N-acetylglucosamine-3-O-acyltransferase (UDP-GlcNAc acyltransferase) catalyzes the first step of lipid A biosynthesis (M. S. Anderson and C. R. H. Raetz, J. Biol. Chem. 262:5159–5169, 1987). We...

Solution structure and dynamics of the outer membrane enzyme PagP by NMR

Hwang, Peter M., Choy, Wing-Yiu, Lo, Eileen I., Chen, Lu, Forman-Kay, Julie D., Raetz, Christian R. H., ...

The bacterial outer membrane enzyme PagP transfers a palmitate chain from a phospholipid to lipid A. In a number of pathogenic Gram-negative bacteria, PagP confers resistance to certain cationic...

Cardiolipin Accumulation in the Inner and Outer Membranes of Escherichia coli Mutants Defective in Phosphatidylserine Synthetase

Raetz, Christian R. H., Kantor, Gina D., Nishijima, Masahiro, Newman, Karl F.

Mutants of Escherichia coli defective in phosphatidylserine synthetase (pss) make less phosphatidylethanolamine than normal cells, and they are temperature sensitive for growth. We have isolated a...

Diglyceride Kinase Mutants of Escherichia coli: Inner Membrane Association of 1,2-Diglyceride and Its Relation to Synthesis of Membrane-Derived Oligosaccharides

Raetz, Christian R. H., Newman, Karl F.

Mutants of Escherichia coli defective in diglyceride kinase contain 10 to 20 times more sn-1,2-diglyceride than normal cells. This material constitutes about 8% of the total lipid in such strains. We...

Transfer of palmitate from phospholipids to lipid A in outer membranes of Gram-negative bacteria

Bishop, Russell E., Gibbons, Henry S., Guina, Tina, Trent, M.Stephen, Miller, Samuel I., Raetz, Christian R.H.

Regulated covalent modifications of lipid A are implicated in virulence of pathogenic Gram-negative bacteria. The Salmonella typhimurium PhoP/PhoQ-activated gene pagP is required both for...

Molecular Validation of LpxC as an Antibacterial Drug Target in Pseudomonas aeruginosa

Mdluli, Khisimuzi E., Witte, Pamela R., Kline, Toni, Barb, Adam W., Erwin, Alice L., Mansfield, Bryce E., ...

LpxC [UDP-3-O-(R-3-hydroxymyristoyl)-GlcNAc deacetylase] is a metalloamidase that catalyzes the first committed step in the biosynthesis of the lipid A component of lipopolysaccharide. A previous...

Structure of UDP-N-acetylglucosamine acyltransferase with a bound antibacterial pentadecapeptide

Williams, Allison H., Immormino, Robert M., Gewirth, Daniel T., Raetz, Christian R. H.

UDP-GlcNAc acyltransferase (LpxA) catalyzes the first step of lipid A biosynthesis, the transfer of the R-3-hydroxyacyl chain from R-3-hydroxyacyl acyl carrier protein (ACP) to the glucosamine 3-OH...

LMSD: LIPID MAPS structure database

Sud, Manish, Fahy, Eoin, Cotter, Dawn, Brown, Alex, Dennis, Edward A., Glass, Christopher K., ...

The LIPID MAPS Structure Database (LMSD) is a relational database encompassing structures and annotations of biologically relevant lipids. Structures of lipids in the database come from four sources:...

Attenuated virulence of a Francisella mutant lacking the lipid A 4′-phosphatase

Wang, Xiaoyuan, Ribeiro, Anthony A., Guan, Ziqiang, Abraham, Soman N., Raetz, Christian R. H.

Francisella tularensis causes tularemia, a highly contagious disease of animals and humans, but the virulence features of F. tularensis are poorly defined. F. tularensis and the related mouse...

Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferase

Williams, Allison H., Raetz, Christian R. H.

UDP-N-acetylglucosamine (UDP-GlcNAc) acyltransferase (LpxA) catalyzes the first step of lipid A biosynthesis, the reversible transfer of the R-3-hydroxyacyl chain from R-3-hydroxyacyl acyl carrier...

Structure of the deacetylase LpxC bound to the antibiotic CHIR-090: Time-dependent inhibition and specificity in ligand binding

Barb, Adam W., Jiang, Ling, Raetz, Christian R. H., Zhou, Pei

The UDP-3-O-(R-3-hydroxyacyl)-N-acetylglucosamine deacetylase LpxC is an essential enzyme of lipid A biosynthesis in Gram-negative bacteria and a promising antibiotic target. CHIR-090, the most...

Crystallization and preliminary X-ray diffraction analysis of phospholipid-bound Sfh1p, a member of the Saccharomyces cerevisiae Sec14p-like phosphatidylinositol transfer protein family

Schaaf, Gabriel, Betts, Laurie, Garrett, Teresa A., Raetz, Christian R. H., Bankaitis, Vytas A.

Yeast Sfh1p, a close homolog of the Sec14p phosphatidylinositol transfer protein, was crystallized in the absence of detergent. X-ray data have been collected to 2.5 Å.

Dolichyl-Phosphate-Glucose Is Used To Make O-Glycans on Glycoproteins of Trichomonas vaginalis▿ †

Grabińska, Kariona A., Ghosh, Sudip K., Guan, Ziqiang, Cui, Jike, Raetz, Christian R. H., Robbins, Phillips W., ...

Trichomonas vaginalis, the protist that causes vaginal itching, has a huge genome with numerous gene duplications. Recently we found that Trichomonas has numerous genes encoding putative...

Periplasmic orientation of nascent lipid A in the inner membrane of an Escherichia coli LptA mutant

Ma, Bing, Reynolds, C. Michael, Raetz, Christian R. H.

The core-lipid A domain of Escherichia coli lipopolysaccharide (LPS) is synthesized on the inner surface of the inner membrane (IM) and flipped to its outer surface by the ABC transporter MsbA....

Active-site architecture and catalytic mechanism of the lipid A deacylase LpxR of Salmonella typhimurium

Rutten, Lucy, Stead, Christopher M., Raetz, Christian R. H., Reynolds, C. Michael, ...

The lipid A portion of lipopolysaccharide, the major component of the outer leaflet of the outer membrane of Gram-negative bacteria, is toxic to humans. Modification of lipid A by enzymes often...