5xw7
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Crystal structure of the flexible tandem repeat domain of bacterial cellulose synthase subunit C== | |
+ | <StructureSection load='5xw7' size='340' side='right' caption='[[5xw7]], [[Resolution|resolution]] 3.27Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[5xw7]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XW7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XW7 FirstGlance]. <br> | ||
+ | </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=5xw7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xw7 OCA], [http://pdbe.org/5xw7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xw7 RCSB], [http://www.ebi.ac.uk/pdbsum/5xw7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xw7 ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Bacterial cellulose (BC) is synthesized and exported through the cell membrane via a large protein complex (terminal complex) that consists of three or four subunits. BcsC is a little-studied subunit considered to export BC to the extracellular matrix. It is predicted to have two domains: a tetratrico peptide repeat (TPR) domain and a beta-barrelled outer membrane domain. Here we report the crystal structure of the N-terminal part of BcsC-TPR domain (Asp24-Arg272) derived from Enterobacter CJF-002. Unlike most TPR-containing proteins which have continuous TPR motifs, this structure has an extra alpha-helix between two clusters of TPR motifs. Five independent molecules in the crystal had three different conformations that varied at the hinge of the inserted alpha-helix. Such structural feature indicates that the inserted alpha-helix confers flexibility to the chain and changes the direction of the TPR super-helix, which was also suggested by structural analysis of BcsC-TPR (Asp24-Leu664) in solution by size exclusion chromatography-small-angle X-ray scattering. The flexibility at the alpha-helical hinge may play important role for exporting glucan chains. | ||
- | + | Crystal structure of the flexible tandem repeat domain of bacterial cellulose synthesis subunit C.,Nojima S, Fujishima A, Kato K, Ohuchi K, Shimizu N, Yonezawa K, Tajima K, Yao M Sci Rep. 2017 Oct 12;7(1):13018. doi: 10.1038/s41598-017-12530-0. PMID:29026093<ref>PMID:29026093</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
+ | <div class="pdbe-citations 5xw7" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Kato, K]] | ||
+ | [[Category: Nojima, S]] | ||
+ | [[Category: Yao, M]] | ||
+ | [[Category: Biosynthetic protein]] | ||
+ | [[Category: Cellulose synthase]] | ||
+ | [[Category: Tetratrico peptide repeat]] |
Revision as of 06:02, 1 November 2017
Crystal structure of the flexible tandem repeat domain of bacterial cellulose synthase subunit C
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