Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ko TP, Tseng ST, Lai SJ, Chen SC, Guan HH, Yang CS, Chen CJ, Chen Y. SH3-Like Motif-Containing C-terminal Domain of Staphylococcal Teichoic Acid Transporter Suggests Possible Function. Proteins. 2016 May 23. doi: 10.1002/prot.25074. PMID:27213893 doi:http://dx.doi.org/10.1002/prot.25074
