2eav
From Proteopedia
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'''Crystal structure of the C-terminal peptidoglycan-binding domain of human peptidoglycan recognition protein Ibeta''' | '''Crystal structure of the C-terminal peptidoglycan-binding domain of human peptidoglycan recognition protein Ibeta''' | ||
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[[Category: Cho, S.]] | [[Category: Cho, S.]] | ||
[[Category: Mariuzza, R A.]] | [[Category: Mariuzza, R A.]] | ||
| - | [[Category: | + | [[Category: Alpha/beta mix]] |
| - | [[Category: | + | [[Category: Sugar binding protein]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 02:15:14 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 23:15, 3 May 2008
Crystal structure of the C-terminal peptidoglycan-binding domain of human peptidoglycan recognition protein Ibeta
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.
About this Structure
2EAV 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 Sun May 4 02:15:14 2008
