4xcm

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==Crystal structure of the putative NlpC/P60 D,L endopeptidase from T. thermophilus==
==Crystal structure of the putative NlpC/P60 D,L endopeptidase from T. thermophilus==
<StructureSection load='4xcm' size='340' side='right' caption='[[4xcm]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
<StructureSection load='4xcm' size='340' side='right' caption='[[4xcm]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
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<table><tr><td colspan='2'>[[4xcm]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XCM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XCM FirstGlance]. <br>
<table><tr><td colspan='2'>[[4xcm]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XCM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XCM FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=4xcm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xcm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xcm RCSB], [http://www.ebi.ac.uk/pdbsum/4xcm PDBsum]</span></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=4xcm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xcm OCA], [http://pdbe.org/4xcm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xcm RCSB], [http://www.ebi.ac.uk/pdbsum/4xcm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xcm ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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LysM domains, which are frequently present as repetitive entities in both bacterial and plant proteins, are known to interact with carbohydrates containing N-acetylglucosamine (GlcNAc) moieties, such as chitin and peptidoglycan. In bacteria, the functional significance of the involvement of multiple LysM domains in substrate binding has so far lacked support from high-resolution structures of ligand-bound complexes. Here, a structural study of the Thermus thermophilus NlpC/P60 endopeptidase containing two LysM domains is presented. The crystal structure and small-angle X-ray scattering solution studies of this endopeptidase revealed the presence of a homodimer. The structure of the two LysM domains co-crystallized with N-acetyl-chitohexaose revealed a new intermolecular binding mode that may explain the differential interaction between LysM domains and short or long chitin oligomers. By combining the structural information with the three-dimensional model of peptidoglycan, a model suggesting how protein dimerization enhances the recognition of peptidoglycan is proposed.
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An intermolecular binding mechanism involving multiple LysM domains mediates carbohydrate recognition by an endopeptidase.,Wong JE, Midtgaard SR, Gysel K, Thygesen MB, Sorensen KK, Jensen KJ, Stougaard J, Thirup S, Blaise M Acta Crystallogr D Biol Crystallogr. 2015 Mar 1;71(Pt 3):592-605. doi:, 10.1107/S139900471402793X. Epub 2015 Feb 26. PMID:25760608<ref>PMID:25760608</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4xcm" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Revision as of 06:32, 26 July 2016

Crystal structure of the putative NlpC/P60 D,L endopeptidase from T. thermophilus

4xcm, resolution 2.65Å

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