1kvm: Difference between revisions

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[[Image:1kvm.gif|left|200px]]
{{Seed}}
[[Image:1kvm.png|left|200px]]


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{{STRUCTURE_1kvm|  PDB=1kvm  |  SCENE=  }}  
{{STRUCTURE_1kvm|  PDB=1kvm  |  SCENE=  }}  


'''X-ray Crystal Structure of AmpC WT beta-Lactamase in Complex with Covalently Bound Cephalothin'''
===X-ray Crystal Structure of AmpC WT beta-Lactamase in Complex with Covalently Bound Cephalothin===




==Overview==
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Beta-lactamases hydrolyze beta-lactam antibiotics and are the leading cause of bacterial resistance to these drugs. Although beta-lactamases have been extensively studied, structures of the substrate-enzyme and product-enzyme complexes have proven elusive. Here, the structure of a mutant AmpC in complex with the beta-lactam cephalothin in its substrate and product forms was determined by X-ray crystallography to 1.53 A resolution. The acyl-enzyme intermediate between AmpC and cephalothin was determined to 2.06 A resolution. The ligand undergoes a dramatic conformational change as the reaction progresses, with the characteristic six-membered dihydrothiazine ring of cephalothin rotating by 109 degrees. These structures correspond to all three intermediates along the reaction path and provide insight into substrate recognition, catalysis, and product expulsion.
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{{ABSTRACT_PUBMED_12005439}}


==About this Structure==
==About this Structure==
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[[Category: Beta-lactamase]]
[[Category: Beta-lactamase]]
[[Category: Cephalothin]]
[[Category: Cephalothin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:05:59 2008''

Revision as of 08:06, 2 July 2008

File:1kvm.png

Template:STRUCTURE 1kvm

X-ray Crystal Structure of AmpC WT beta-Lactamase in Complex with Covalently Bound Cephalothin

Template:ABSTRACT PUBMED 12005439

About this Structure

1KVM is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structural milestones in the reaction pathway of an amide hydrolase: substrate, acyl, and product complexes of cephalothin with AmpC beta-lactamase., Beadle BM, Trehan I, Focia PJ, Shoichet BK, Structure. 2002 Mar;10(3):413-24. PMID:12005439

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