3NY4

Crystal Structure of BlaC-K73A bound with Cefamandole

3NY4 の概要

• エントリーDOI: 10.2210/pdb3ny4/pdb
• 分子名称: 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)
• 機能のキーワード: penicillin binding protein, beta-lactam complex, hydrolase-antibiotic complex, hydrolase/antibiotic
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30622.11

構造登録者

Tremblay, L.W.,Blanchard, J.S. (登録日: 2010-07-14, 公開日: 2010-11-24, 最終更新日: 2024-02-21)

主引用文献

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

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: 20961112
DOI: 10.1021/bi1015088

実験手法

X-RAY DIFFRACTION (1.22 Å)