1ceg: Difference between revisions

Revision as of 20:38, 30 June 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:1ceg.png

Template:STRUCTURE 1ceg

CEPHALOTHIN COMPLEXED WITH DD-PEPTIDASECEPHALOTHIN COMPLEXED WITH DD-PEPTIDASE

Template:ABSTRACT PUBMED 7626623

About this StructureAbout this Structure

1CEG is a Single protein structure of sequence from Streptomyces sp.. Full crystallographic information is available from OCA.

ReferenceReference

Binding of cephalothin and cefotaxime to D-ala-D-ala-peptidase reveals a functional basis of a natural mutation in a low-affinity penicillin-binding protein and in extended-spectrum beta-lactamases., Kuzin AP, Liu H, Kelly JA, Knox JR, Biochemistry. 1995 Jul 25;34(29):9532-40. PMID:7626623

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''CEPHALOTHIN COMPLEXED WITH DD-PEPTIDASE'''
+===CEPHALOTHIN COMPLEXED WITH DD-PEPTIDASE===
-==Overview==
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-Two clinically-important beta-lactam antibiotics, cephalothin and cefotaxime, have been observed by X-ray crystallography bound to the reactive Ser62 of the D-alanyl-D-alanine carboxypeptidase/transpeptidase of Streptomyces sp. R61. Refinement of the two crystal structures produced R factors for 3 sigma (F) data of 0.166 (to 1.8 A) and 0.170 (to 2.0 A) for the cephalothin and cefotaxime complexes, respectively. In each complex, a water molecule is within 3.1 and 3.6 A of the acylated beta-lactam carbonyl carbon atom, but is poorly activated by active site residues for nucleophilic attack and deacylation. This apparent lack of good stereochemistry for facile hydrolysis is in accord with the long half-lives of cephalosporin intermediates in solution (20-40 h) and the efficacy of these beta-lactams as inhibitors of bacterial cell wall synthesis. Different hydrogen binding patterns of the two cephalosporins to Thr301 are consistent with the low cefotaxime affinity of an altered penicillin-binding protein, PBP-2x, reported in cefotaxime-resistant strains of Streptococcus pneumoniae, and with the ability of mutant class A beta-lactamases to hydrolyze third-generation cephalosporins.
+The line below this paragraph, {{ABSTRACT_PUBMED_7626623}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_7626623}}
 ==About this Structure==
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 [[Category: Hydrolase-transpeptidase]]
 [[Category: Penicillin target]]
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