1ll5: Difference between revisions
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'''X-ray crystal structure of AmpC WT beta-lactamase in complex with covalently bound imipenem''' | '''X-ray crystal structure of AmpC WT beta-lactamase in complex with covalently bound imipenem''' | ||
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[[Category: Beadle, B M.]] | [[Category: Beadle, B M.]] | ||
[[Category: Shoichet, B K.]] | [[Category: Shoichet, B K.]] | ||
[[Category: | [[Category: Beta-lactamase]] | ||
[[Category: | [[Category: Carbapenem]] | ||
[[Category: | [[Category: Imipenem]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:01:42 2008'' | |||
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Revision as of 00:01, 3 May 2008
X-ray crystal structure of AmpC WT beta-lactamase in complex with covalently bound imipenem
OverviewOverview
To determine how imipenem inhibits the class C beta-lactamase AmpC, the X-ray crystal structure of the acyl-enzyme complex was determined to a resolution of 1.80 A. In the complex, the lactam carbonyl oxygen of imipenem has flipped by approximately 180 degrees compared to its expected position; the electrophilic acyl center is thus displaced from the point of hydrolytic attack. This conformation resembles that of imipenem bound to the class A enzyme TEM-1 but is different from that of moxalactam bound to AmpC.
About this StructureAbout this Structure
1LL5 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for imipenem inhibition of class C beta-lactamases., Beadle BM, Shoichet BK, Antimicrob Agents Chemother. 2002 Dec;46(12):3978-80. PMID:12435704 Page seeded by OCA on Sat May 3 00:01:42 2008