5j72

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'''Unreleased structure'''
 
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The entry 5j72 is ON HOLD until Paper Publication
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==Cwp6 from Clostridium difficile==
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<StructureSection load='5j72' size='340' side='right' caption='[[5j72]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5j72]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J72 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J72 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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acetylmuramoyl-L-alanine_amidase N-acetylmuramoyl-L-alanine amidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.28 3.5.1.28] </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=5j72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j72 OCA], [http://pdbe.org/5j72 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j72 RCSB], [http://www.ebi.ac.uk/pdbsum/5j72 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j72 ProSAT]</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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Bacterial cell wall proteins play crucial roles in cell survival, growth, and environmental interactions. In Gram-positive bacteria, cell wall proteins include several types that are non-covalently attached via cell wall binding domains. Of the two conserved surface-layer (S-layer)-anchoring modules composed of three tandem SLH or CWB2 domains, the latter have so far eluded structural insight. The crystal structures of Cwp8 and Cwp6 reveal multi-domain proteins, each containing an embedded CWB2 module. It consists of a triangular trimer of Rossmann-fold CWB2 domains, a feature common to 29 cell wall proteins in Clostridium difficile 630. The structural basis of the intact module fold necessary for its binding to the cell wall is revealed. A comparison with previously reported atomic force microscopy data of S-layers suggests that C. difficile S-layers are complex oligomeric structures, likely composed of several different proteins.
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Authors:
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The CWB2 Cell Wall-Anchoring Module Is Revealed by the Crystal Structures of the Clostridium difficile Cell Wall Proteins Cwp8 and Cwp6.,Usenik A, Renko M, Mihelic M, Lindic N, Borisek J, Perdih A, Pretnar G, Muller U, Turk D Structure. 2017 Mar 7;25(3):514-521. doi: 10.1016/j.str.2016.12.018. Epub 2017, Jan 26. PMID:28132783<ref>PMID:28132783</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5j72" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: N-acetylmuramoyl-L-alanine amidase]]
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[[Category: Renko, M]]
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[[Category: Turk, D]]
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[[Category: Usenik, A]]
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[[Category: Amidase_3]]
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[[Category: Cell wall protein]]
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[[Category: Cwb2 domain]]
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[[Category: Hydrolase]]
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[[Category: S-layer]]

Revision as of 07:29, 9 March 2017

Cwp6 from Clostridium difficile

5j72, resolution 1.70Å

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