5bnd

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5bnd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bnd OCA], [https://pdbe.org/5bnd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bnd RCSB], [https://www.ebi.ac.uk/pdbsum/5bnd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bnd ProSAT]</span></td></tr>

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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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