1zat

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1zat.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1zat.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1zat| PDB=1zat | SCENE= }}
{{STRUCTURE_1zat| PDB=1zat | SCENE= }}
-
'''Crystal Structure of an Enterococcus faecium peptidoglycan binding protein at 2.4 A resolution'''
+
===Crystal Structure of an Enterococcus faecium peptidoglycan binding protein at 2.4 A resolution===
-
==Overview==
+
<!--
-
During the final stages of cell-wall synthesis in bacteria, penicillin-binding proteins (PBPs) catalyse the cross-linking of peptide chains from adjacent glycan strands of nascent peptidoglycan. We have recently shown that this step can be bypassed by an L,D-transpeptidase, which confers high-level beta-lactam-resistance in Enterococcus faecium. The resistance bypass leads to replacement of D-Ala4--&gt;D-Asx-L-Lys3 cross-links generated by the PBPs by L-Lys3--&gt;D-Asx-L-Lys3 cross-links generated by the L,D-transpeptidase. As the first structure of a member of this new transpeptidase family, we have determined the crystal structure of a fragment of the L,D-transpeptidase from E.faecium (Ldt(fm217)) at 2.4A resolution. Ldt(fm217) consists of two domains, the N-terminal domain, a new mixed alpha-beta fold, and the ErfK_YbiS_YhnG C-terminal domain, a representative of the mainly beta class of protein structures. Residue Cys442 of the C-terminal domain has been proposed to be the catalytic residue implicated in the cleavage of the L-Lys-D-Ala peptide bond. Surface analysis of Ldt(fm217) reveals that residue Cys442 is localized in a buried pocket and is accessible by two paths on different sides of the protein. We propose that the two paths to the catalytic residue Cys442 are the binding sites for the acceptor and donor substrates of the L,D-transpeptidase.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16647082}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16647082 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16647082}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: L,d-transpeptidation]]
[[Category: L,d-transpeptidation]]
[[Category: Peptidoglycan]]
[[Category: Peptidoglycan]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:23:53 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 10:02:16 2008''

Revision as of 07:02, 29 July 2008

Image:1zat.png

Template:STRUCTURE 1zat

Crystal Structure of an Enterococcus faecium peptidoglycan binding protein at 2.4 A resolution

Template:ABSTRACT PUBMED 16647082

About this Structure

1ZAT is a Single protein structure of sequence from Enterococcus faecium. Full crystallographic information is available from OCA.

Reference

Crystal structure of a novel beta-lactam-insensitive peptidoglycan transpeptidase., Biarrotte-Sorin S, Hugonnet JE, Delfosse V, Mainardi JL, Gutmann L, Arthur M, Mayer C, J Mol Biol. 2006 Jun 9;359(3):533-8. Epub 2006 Mar 23. PMID:16647082

Page seeded by OCA on Tue Jul 29 10:02:16 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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