3NY4
Crystal Structure of BlaC-K73A bound with Cefamandole
Summary for 3NY4
| Entry DOI | 10.2210/pdb3ny4/pdb |
| Descriptor | Beta-lactamase, PHOSPHATE ION, (6R,7R)-7-{[(2R)-2-hydroxy-2-phenylacetyl]amino}-3-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, ... (4 entities in total) |
| Functional Keywords | penicillin binding protein, beta-lactam complex, hydrolase-antibiotic complex, hydrolase/antibiotic |
| Biological source | Mycobacterium tuberculosis |
| Total number of polymer chains | 1 |
| Total formula weight | 30622.11 |
| Authors | Tremblay, L.W.,Blanchard, J.S. (deposition date: 2010-07-14, release date: 2010-11-24, Last modification date: 2024-02-21) |
| Primary citation | Tremblay, L.W.,Xu, H.,Blanchard, J.S. Structures of the Michaelis Complex (1.2 A) and the Covalent Acyl Intermediate (2.0 A) of Cefamandole Bound in the Active Sites of the Mycobacterium tuberculosis beta-Lactamase K73A and E166A Mutants. Biochemistry, 49:9685-9687, 2010 Cited by PubMed Abstract: The genome of Mycobacterium tuberculosis (TB) contains a gene that encodes a highly active β-lactamase, BlaC, that imparts TB with resistance to β-lactam chemotherapy. The structure of covalent BlaC-β-lactam complexes suggests that active site residues K73 and E166 are essential for acylation and deacylation, respectively. We have prepared the K73A and E166A mutant forms of BlaC and have determined the structures of the Michaelis complex of cefamandole and the covalently bound acyl intermediate of cefamandole at resolutions of 1.2 and 2.0 Å, respectively. These structures provide insight into the details of the catalytic mechanism. PubMed: 20961112DOI: 10.1021/bi1015088 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.22 Å) |
Structure validation
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