2eax

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[[Image:2eax.gif|left|200px]]<br /><applet load="2eax" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2eax.gif|left|200px]]
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caption="2eax, resolution 2.10&Aring;" />
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'''Crystal structure of human PGRP-IBETAC in complex with glycosamyl muramyl pentapeptide'''<br />
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{{Structure
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|PDB= 2eax |SIZE=350|CAPTION= <scene name='initialview01'>2eax</scene>, resolution 2.10&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> and <scene name='pdbligand=MMR:N-((2R,3R,4S,6S)-6-(HYDROXYMETHYL)-2-METHOXY-4-((S)-1-OXOPROPAN-2-YLOXY)TETRAHYDRO-2H-PYRAN-3-YL)ETHANAMIDE'>MMR</scene>
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|ACTIVITY=
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|GENE= PGRPIB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''Crystal structure of human PGRP-IBETAC in complex with glycosamyl muramyl pentapeptide'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2EAX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=MMR:'>MMR</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EAX OCA].
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2EAX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EAX OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17502600 17502600]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17502600 17502600]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: sugar binding protein]]
[[Category: sugar binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:08:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:37:42 2008''

Revision as of 14:37, 20 March 2008

Image:2eax.gif


PDB ID 2eax

Drag the structure with the mouse to rotate
, resolution 2.10Å
Ligands: and
Gene: PGRPIB (Homo sapiens)
Coordinates: save as pdb, mmCIF, xml



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.

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

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