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3cg5

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{{STRUCTURE_3cg5| PDB=3cg5 | SCENE= }}
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'''Crystal Structure of the Covalent Adduct Formed between TB B-lactamase and Clavulanate'''
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===Crystal Structure of the Covalent Adduct Formed between TB B-lactamase and Clavulanate===
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==Overview==
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The intrinsic resistance of Mycobacterium tuberculosis to the beta-lactam class of antibiotics arises from a chromosomally encoded, extended spectrum, class A beta-lactamase, BlaC. Herein, we report the X-ray crystallographic structure of BlaC inhibited with clavulanate at a resolution of 1.7 A with an R-factor value of 0.180 and R-free value of 0.212 for the m/ z +154 clavulanate-derived fragment observed in the active site. Structural evidence reveals the presence of hydrogen bonds to the C1 carbonyl along with a coplanar arrangement of C1, C2, C3, and N4, which favors enolization to generate a trans-alpha,beta-eneamine, stabilizing the +154 adduct from hydrolysis. The irreversible inhibition of BlaC suggests that treatment of M. tuberculosis with a combination of a beta-lactam antibiotic and clavulanate may lead to rapid bactericidal activity.
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==About this Structure==
==About this Structure==
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 28 09:21:52 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:49:58 2008''

Revision as of 14:50, 27 July 2008

Image:3cg5.png

Template:STRUCTURE 3cg5

Crystal Structure of the Covalent Adduct Formed between TB B-lactamase and Clavulanate

Template:ABSTRACT PUBMED 18422342

About this Structure

3CG5 is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

Structure of the covalent adduct formed between Mycobacterium tuberculosis beta-lactamase and clavulanate., Tremblay LW, Hugonnet JE, Blanchard JS, Biochemistry. 2008 May 13;47(19):5312-6. Epub 2008 Apr 19. PMID:18422342

Page seeded by OCA on Sun Jul 27 17:49:58 2008

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