1cef

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1cef.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1cef.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1cef| PDB=1cef | SCENE= }}
{{STRUCTURE_1cef| PDB=1cef | SCENE= }}
-
'''CEFOTAXIME COMPLEXED WITH THE STREPTOMYCES R61 DD-PEPTIDASE'''
+
===CEFOTAXIME COMPLEXED WITH THE STREPTOMYCES R61 DD-PEPTIDASE===
-
==Overview==
+
<!--
-
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
 +
(as it appears on PubMed at http://www.pubmed.gov), where 7626623 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_7626623}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Hydrolase-transpeptidase]]
[[Category: Hydrolase-transpeptidase]]
[[Category: Penicillin target]]
[[Category: Penicillin target]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:38:23 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:37:57 2008''

Revision as of 17:37, 30 June 2008

Image:1cef.png

Template:STRUCTURE 1cef

CEFOTAXIME COMPLEXED WITH THE STREPTOMYCES R61 DD-PEPTIDASE

Template:ABSTRACT PUBMED 7626623

About this Structure

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

Reference

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

Page seeded by OCA on Mon Jun 30 20:37:57 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1cef"
Personal tools