1qme: Difference between revisions

Revision as of 09:31, 29 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:1qme.png

Template:STRUCTURE 1qme

PENICILLIN-BINDING PROTEIN 2X (PBP-2X)PENICILLIN-BINDING PROTEIN 2X (PBP-2X)

Template:ABSTRACT PUBMED 10860753

About this StructureAbout this Structure

1QME is a Single protein structure of sequence from Streptococcus pneumoniae. Full crystallographic information is available from OCA.

ReferenceReference

The crystal structure of the penicillin-binding protein 2x from Streptococcus pneumoniae and its acyl-enzyme form: implication in drug resistance., Gordon E, Mouz N, Duee E, Dideberg O, J Mol Biol. 2000 Jun 2;299(2):477-85. PMID:10860753

Page seeded by OCA on Tue Jul 29 09:31:20 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1qme.jpg|left|200px]]
+{{Seed}}
+[[Image:1qme.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1qme|  PDB=1qme  |  SCENE=  }}
-'''PENICILLIN-BINDING PROTEIN 2X (PBP-2X)'''
+===PENICILLIN-BINDING PROTEIN 2X (PBP-2X)===
-==Overview==
+<!--
-Penicillin-binding proteins (PBPs), the primary targets for beta-lactam antibiotics, are periplasmic membrane-attached proteins responsible for the construction and maintenance of the bacterial cell wall. Bacteria have developed several mechanisms of resistance, one of which is the mutation of the target enzymes to reduce their affinity for beta-lactam antibiotics. Here, we describe the structure of PBP2x from Streptococcus pneumoniae determined to 2.4 A. In addition, we also describe the PBP2x structure in complex with cefuroxime, a therapeutically relevant antibiotic, at 2.8 A. Surprisingly, two antibiotic molecules are observed: one as a covalent complex with the active-site serine residue, and a second one between the C-terminal and the transpeptidase domains. The structure of PBP2x reveals an active site similar to those of the class A beta-lactamases, albeit with an absence of unambiguous deacylation machinery. The structure highlights a few amino acid residues, namely Thr338, Thr550 and Gln552, which are directly related to the resistance phenomenon.
+The line below this paragraph, {{ABSTRACT_PUBMED_10860753}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10860753 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10860753}}
 ==About this Structure==
@@ Line 30: / Line 34: @@
 [[Category: Resistance]]
 [[Category: Transmembrane]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 06:26:57 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:31:20 2008''