4gf9

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{{STRUCTURE_4gf9| PDB=4gf9 | SCENE= }}
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==Structural insights into the dual strategy of recognition of peptidoglycan recognition protein, PGRP-S: ternary complex of PGRP-S with LPS and fatty acid==
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===Structural insights into the dual strategy of recognition of peptidoglycan recognition protein, PGRP-S: ternary complex of PGRP-S with LPS and fatty acid===
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<StructureSection load='4gf9' size='340' side='right' caption='[[4gf9]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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{{ABSTRACT_PUBMED_23326499}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4gf9]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Camelus_dromedarius Camelus dromedarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GF9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GF9 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LP5:(R)-((2R,3S,4R,5R,6R)-3-HYDROXY-2-(HYDROXYMETHYL)-5-((R)-3-HYDROXYTETRADECANAMIDO)-6-(PHOSPHONOOXY)TETRAHYDRO-2H-PYRAN-4-YL)+3-HYDROXYTETRADECANOATE'>LP5</scene>, <scene name='pdbligand=STE:STEARIC+ACID'>STE</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4gf9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gf9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gf9 RCSB], [http://www.ebi.ac.uk/pdbsum/4gf9 PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Peptidoglycan recognition proteins (PGRPs) are part of the innate immune system. The 19 kDa Short PGRP (PGRP-S) is one of the four mammalian PGRPs. The concentration of PGRP-S in camel (CPGRP-S) has been shown to increase considerably during mastitis. The structure of CPGRP-S consists of four protein molecules designated as A, B, C and D forming stable intermolecular contacts, A-B and C-D. The A-B and C-D interfaces are located on the opposite sides of the same monomer leading to the the formation of a linear chain with alternating A-B and C-D contacts. Two ligand binding sites, one at C-D contact and another at A-B contact have been observed. CPGRP-S binds to the components of bacterial cell wall molecules such as lipopolysaccharide (LPS), lipoteichoic acid (LTA), and peptidoglycan (PGN) from both gram-positive and gram-negative bacteria. It also binds to fatty acids including mycolic acid of the Mycobacterium tuberculosis (Mtb). Previous structural studies of binary complexes of CPGRP-S with LPS and stearic acid (SA) have shown that LPS binds to CPGRP-S at C-D contact (Site-1) while SA binds to it at the A-B contact (Site-2). The binding studies using surface plasmon resonance showed that LPS and SA bound to CPGRP-S in the presence of each other. The structure determination of the ternary complex showed that LPS and SA bound to CPGRP-S at Site-1 and Site-2 respectively. LPS formed 13 hydrogen bonds and 159 van der Waals contacts (distances &lt;/=4.2 A) while SA formed 56 van der Waals contacts. The ELISA test showed that increased levels of productions of pro-inflammatory cytokines TNF-alpha and IFN-gamma due to LPS and SA decreased considerably upon the addition of CPGRP-S.
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==Function==
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Structural insights into the dual strategy of recognition by peptidoglycan recognition protein, PGRP-S: structure of the ternary complex of PGRP-S with lipopolysaccharide and stearic acid.,Sharma P, Dube D, Sinha M, Yadav S, Kaur P, Sharma S, Singh TP PLoS One. 2013;8(1):e53756. doi: 10.1371/journal.pone.0053756. Epub 2013 Jan 9. PMID:23326499<ref>PMID:23326499</ref>
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[[http://www.uniprot.org/uniprot/PGRP1_CAMDR PGRP1_CAMDR]] Pattern receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria. Has bactericidal activity towards Gram-positive bacteria. May kill Gram-positive bacteria by interfering with peptidoglycan biosynthesis. Binds also to Gram-negative bacteria. Involved in innate immunity. Is microbicidal for Gram-positive and Gram-negative bacteria and yeast. May function in intracellular killing of bacteria (By similarity).
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[4gf9]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Camelus_dromedarius Camelus dromedarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GF9 OCA].
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</div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Camelus dromedarius]]
[[Category: Camelus dromedarius]]
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[[Category: Dube, D.]]
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[[Category: Dube, D]]
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[[Category: Kaur, P.]]
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[[Category: Kaur, P]]
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[[Category: Sharma, P.]]
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[[Category: Sharma, P]]
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[[Category: Sharma, S.]]
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[[Category: Sharma, S]]
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[[Category: Singh, T P.]]
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[[Category: Singh, T P]]
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[[Category: Sinha, M.]]
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[[Category: Sinha, M]]
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[[Category: Yadav, S.]]
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[[Category: Yadav, S]]
[[Category: Antibiotic]]
[[Category: Antibiotic]]
[[Category: Antimicrobial]]
[[Category: Antimicrobial]]

Revision as of 11:27, 21 December 2014

Structural insights into the dual strategy of recognition of peptidoglycan recognition protein, PGRP-S: ternary complex of PGRP-S with LPS and fatty acid

4gf9, resolution 2.80Å

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