5bnd
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the C-terminal domain of TagH== | |
| + | <StructureSection load='5bnd' size='340' side='right' caption='[[5bnd]], [[Resolution|resolution]] 2.68Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5bnd]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BND OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BND 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=5bnd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bnd OCA], [http://pdbe.org/5bnd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bnd RCSB], [http://www.ebi.ac.uk/pdbsum/5bnd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5bnd ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The negatively charged bacterial polysaccharides - wall teichoic acids (WTAs) are synthesized intracellularly and exported by a two-component transporter, TagGH, comprising a transmembrane subunit TagG and an ATPase subunit TagH. We determined the crystal structure of the C-terminal domain of TagH (TagH-C) to investigate its function. The structure shows an N-terminal SH3-like subdomain wrapped by a C-terminal subdomain with an anti-parallel beta-sheet and an outer shell of alpha-helices. A stretch of positively charged surface across the subdomain interface is flanked by two negatively charged regions, suggesting a potential binding site for negatively charged polymers, such as WTAs or acidic peptide chains. This article is protected by copyright. All rights reserved. | ||
| - | + | SH3-Like Motif-Containing C-terminal Domain of Staphylococcal Teichoic Acid Transporter Suggests Possible Function.,Ko TP, Tseng ST, Lai SJ, Chen SC, Guan HH, Yang CS, Chen CJ, Chen Y Proteins. 2016 May 23. doi: 10.1002/prot.25074. PMID:27213893<ref>PMID:27213893</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5bnd" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Chen, S C]] | ||
[[Category: Chen, Y]] | [[Category: Chen, Y]] | ||
| - | [[Category: | + | [[Category: Transport protein]] |
| + | [[Category: Transporter]] | ||
Revision as of 02:17, 13 July 2016
Crystal structure of the C-terminal domain of TagH
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