This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2eax

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2eax.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2eax.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2eax| PDB=2eax | SCENE= }}
{{STRUCTURE_2eax| PDB=2eax | SCENE= }}
-
'''Crystal structure of human PGRP-IBETAC in complex with glycosamyl muramyl pentapeptide'''
+
===Crystal structure of human PGRP-IBETAC in complex with glycosamyl muramyl pentapeptide===
-
==Overview==
+
<!--
-
Peptidoglycan recognition proteins (PGRPs) are highly conserved pattern-recognition molecules of the innate immune system that bind bacterial peptidoglycans (PGNs), which are polymers of alternating N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM) cross-linked by short peptide stems. Human PRGPs are bactericidal against pathogenic and nonpathogenic Gram-positive bacteria, but not normal flora bacteria. Like certain glycopeptide antibiotics (e.g., vancomycin), PGRPs kill bacteria by directly interacting with their cell wall PGN, thereby interfering with PGN maturation. To better understand the bactericidal mechanism of PGRPs, we determined the crystal structure of the C-terminal PGN-binding domain of human PGRP-I beta in complex with NAG-NAM-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala, a synthetic glycopeptide comprising a complete PGN repeat. This structure, in conjunction with the previously reported NMR structure of a dimeric PGN fragment, permitted identification of major conformational differences between free and PGRP-bound PGN with respect to the relative orientation of saccharide and peptide moieties. These differences provided structural insights into the bactericidal mechanism of human PGRPs. On the basis of molecular modeling, we propose that these proteins disrupt cell wall maturation not only by sterically encumbering access of biosynthetic enzymes to the nascent PGN chains, but also by locking PGN into a conformation that prevents formation of cross-links between peptide stems in the growing cell wall.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17502600}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17502600 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17502600}}
==About this Structure==
==About this Structure==
Line 25: Line 29:
[[Category: Alpha/beta]]
[[Category: Alpha/beta]]
[[Category: Sugar binding protein]]
[[Category: Sugar binding protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 02:15:25 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:45:04 2008''

Revision as of 06:45, 29 July 2008

Image:2eax.png

Template:STRUCTURE 2eax

Crystal structure of human PGRP-IBETAC in complex with glycosamyl muramyl pentapeptide

Template:ABSTRACT PUBMED 17502600

About this Structure

2EAX is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural insights into the bactericidal mechanism of human peptidoglycan recognition proteins., Cho S, Wang Q, Swaminathan CP, Hesek D, Lee M, Boons GJ, Mobashery S, Mariuzza RA, Proc Natl Acad Sci U S A. 2007 May 22;104(21):8761-6. Epub 2007 May 14. PMID:17502600

Page seeded by OCA on Tue Jul 29 09:45:04 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2eax"
Personal tools