Structural highlights
3ny4 is a 1 chain structure with sequence from "bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , |
| Gene: | blaA, blaC, Rv2068c, MT2128, MTCY49.07c ("Bacillus tuberculosis" (Zopf 1883) Klein 1884) |
| Activity: | Beta-lactamase, with EC number 3.5.2.6 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Publication Abstract from PubMed
The genome of Mycobacterium tuberculosis (TB) contains a gene that encodes a highly active beta-lactamase, BlaC, that imparts TB with resistance to beta-lactam chemotherapy. The structure of covalent BlaC-beta-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 A, respectively. These structures provide insight into the details of the catalytic mechanism.
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 .,Tremblay LW, Xu H, Blanchard JS Biochemistry. 2010 Nov 16;49(45):9685-7. Epub 2010 Oct 25. PMID:20961112[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tremblay LW, Xu H, Blanchard JS. 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. 2010 Nov 16;49(45):9685-7. Epub 2010 Oct 25. PMID:20961112 doi:10.1021/bi1015088
