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-[[Image:1kvl.gif|left|200px]]
+{{Seed}}
+[[Image:1kvl.png|left|200px]]
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 {{STRUCTURE_1kvl|  PDB=1kvl  |  SCENE=  }}
-'''X-ray Crystal Structure of AmpC S64G Mutant beta-Lactamase in Complex with Substrate and Product Forms of Cephalothin'''
+===X-ray Crystal Structure of AmpC S64G Mutant beta-Lactamase in Complex with Substrate and Product Forms of Cephalothin===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12005439}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12005439 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12005439}}
 ==About this Structure==
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 [[Category: Product-enzyme complex]]
 [[Category: Substrate-enzyme complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 23:13:15 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 11:06:01 2008''