1ll9: Difference between revisions

Revision as of 21:22, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1ll9.png

Template:STRUCTURE 1ll9

Crystal Structure Of AmpC beta-Lactamase From E. Coli In Complex With AmoxicillinCrystal Structure Of AmpC beta-Lactamase From E. Coli In Complex With Amoxicillin

Template:ABSTRACT PUBMED 12323371

About this StructureAbout this Structure

1LL9 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Using steric hindrance to design new inhibitors of class C beta-lactamases., Trehan I, Morandi F, Blaszczak LC, Shoichet BK, Chem Biol. 2002 Sep;9(9):971-80. PMID:12323371

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-'''Crystal Structure Of AmpC beta-Lactamase From E. Coli In Complex With Amoxicillin'''
+===Crystal Structure Of AmpC beta-Lactamase From E. Coli In Complex With Amoxicillin===
-==Overview==
+<!--
-beta-lactamases confer resistance to beta-lactam antibiotics such as penicillins and cephalosporins. However, beta-lactams that form an acyl-intermediate with the enzyme but subsequently are hindered from forming a catalytically competent conformation seem to be inhibitors of beta-lactamases. This inhibition may be imparted by specific groups on the ubiquitous R(1) side chain of beta-lactams, such as the 2-amino-4-thiazolyl methoxyimino (ATMO) group common among third-generation cephalosporins. Using steric hindrance of deacylation as a design guide, penicillin and carbacephem substrates were converted into effective beta-lactamase inhibitors and antiresistance antibiotics. To investigate the structural bases of inhibition, the crystal structures of the acyl-adducts of the penicillin substrate amoxicillin and the new analogous inhibitor ATMO-penicillin were determined. ATMO-penicillin binds in a catalytically incompetent conformation resembling that adopted by third-generation cephalosporins, demonstrating the transferability of such sterically hindered groups in inhibitor design.
+The line below this paragraph, {{ABSTRACT_PUBMED_12323371}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_12323371}}
 ==About this Structure==
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 [[Category: Hydrolase]]
 [[Category: Serine]]
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