4uz2
From Proteopedia
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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=4uz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uz2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uz2 RCSB], [http://www.ebi.ac.uk/pdbsum/4uz2 PDBsum]</span></td></tr> | <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=4uz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uz2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uz2 RCSB], [http://www.ebi.ac.uk/pdbsum/4uz2 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 07:56, 26 March 2015
Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus
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