O. Herzberg

Publication List Details

Period

1997 - 2009

Number

15

Co-Authors

Structure and function of 2,3-dimethylmalate lyase, a PEP mutase/isocitrate lyase superfamily member (2009)

Narayanan, B., Niu, W., Joosten, H-J., Li, Z., Kuipers, R.K., Schaap, P.J., ...

The Aspergillus niger genome contains four genes that encode proteins exhibiting greater than 30% amino acid sequence identity to the confirmed oxaloacetate acetyl hydrolase (OAH), an enzyme that...

Swiveling-domain mechanism for enzymatic phosphotransfer between remote reaction sites.

Herzberg, O, Chen, C C, Kapadia, G, McGuire, M, Carroll, L J, Noh, S J, ...

The crystal structure of pyruvate phosphate dikinase, a histidyl multiphosphotransfer enzyme that synthesizes adenosine triphosphate, reveals a three-domain molecule in which the phosphohistidine...

Structure of S-lectin, a developmentally regulated vertebrate beta-galactoside-binding protein.

Liao, D I, Kapadia, G, Ahmed, H, Vasta, G R, Herzberg, O

The crystal structure of a 14-kDa bovine spleen S-lectin complexed with the disaccharide N-acetyllactosamine at 1.9-A resolution reveals a surprising structural relationship to legume lectins,...

Structure of the histidine-containing phosphocarrier protein HPr from Bacillus subtilis at 2.0-A resolution.

Herzberg, O, Reddy, P, Sutrina, S, Saier, M H, Reizer, J, Kapadia, G

The crystal structure of the histidine-containing phosphocarrier protein (HPr) of the phosphoenolpyruvate:sugar phosphotransferase system (PTS) from Bacillus subtilis has been determined at 2.0-A...

Three-dimensional structure of the Escherichia coli phosphocarrier protein IIIglc.

Worthylake, D, Meadow, N D, Roseman, S, Liao, D I, Herzberg, O, Remington, S J

The crystal structure of a proteolytically modified form of the Escherichia coli phosphocarrier and signal transducing protein IIIglc has been determined by multiple isomorphous and molecular...

The crystal structure of beta-lactamase from Staphylococcus aureus at 0.5 nm resolution.

Moult, J, Sawyer, L, Herzberg, O, Jones, C L, Coulson, A F, Green, D W, ...

The preparation, crystallization and low-resolution structure determination of beta-lactamase (EC 3.5.2.6, 'penicillinase') from Staphylococcus aureus is described. The enzyme crystallizes in space...

Swiveling-domain mechanism for enzymatic phosphotransfer between remote reaction sites.

Herzberg, O, Chen, C C, Kapadia, G, McGuire, M, Carroll, L J, Noh, S J, ...

The crystal structure of pyruvate phosphate dikinase, a histidyl multiphosphotransfer enzyme that synthesizes adenosine triphosphate, reveals a three-domain molecule in which the phosphohistidine...

Structure of S-lectin, a developmentally regulated vertebrate beta-galactoside-binding protein.

Liao, D I, Kapadia, G, Ahmed, H, Vasta, G R, Herzberg, O

The crystal structure of a 14-kDa bovine spleen S-lectin complexed with the disaccharide N-acetyllactosamine at 1.9-A resolution reveals a surprising structural relationship to legume lectins,...

Structure of the histidine-containing phosphocarrier protein HPr from Bacillus subtilis at 2.0-A resolution.

Herzberg, O, Reddy, P, Sutrina, S, Saier, M H, Reizer, J, Kapadia, G

The crystal structure of the histidine-containing phosphocarrier protein (HPr) of the phosphoenolpyruvate:sugar phosphotransferase system (PTS) from Bacillus subtilis has been determined at 2.0-A...

Three-dimensional structure of the Escherichia coli phosphocarrier protein IIIglc.

Worthylake, D, Meadow, N D, Roseman, S, Liao, D I, Herzberg, O, Remington, S J

The crystal structure of a proteolytically modified form of the Escherichia coli phosphocarrier and signal transducing protein IIIglc has been determined by multiple isomorphous and molecular...

The crystal structure of beta-lactamase from Staphylococcus aureus at 0.5 nm resolution.

Moult, J, Sawyer, L, Herzberg, O, Jones, C L, Coulson, A F, Green, D W, ...

The preparation, crystallization and low-resolution structure determination of beta-lactamase (EC 3.5.2.6, 'penicillinase') from Staphylococcus aureus is described. The enzyme crystallizes in space...

Crystal structures of the cadmium- and mercury-substituted metallo-beta-lactamase from Bacteroides fragilis.

Concha, N. O., Rasmussen, B. A., Bush, K., Herzberg, O.

The metallo-beta-lactamases require zinc or cadmium for hydrolyzing beta-lactam antibiotics and are inhibited by mercurial compounds. To data, there are no clinically useful inhibitors of this class...

Structural consequences of the active site substitution Cys181 ==> Ser in metallo-beta-lactamase from Bacteroides fragilis.

Li, Z., Rasmussen, B. A., Herzberg, O.

The metallo-beta-lactamases require divalent cations such as zinc or cadmium for hydrolyzing the amide bond of beta-lactam antibiotics. The crystal structure of the Zn2+ -bound enzyme from...