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SH3‐like motif‐containing C‐terminal domain of staphylococcal teichoic acid transporter suggests possible function
Author(s) -
Ko TzuPing,
Tseng ShihTing,
Lai ShuJung,
Chen ShengChia,
Guan HongHsiang,
Shin Yang Chia,
Jung Chen Chun,
Chen Yeh
Publication year - 2016
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.25074
Subject(s) - teichoic acid , chemistry , transmembrane domain , transmembrane protein , protein subunit , c terminus , peptide , peptide sequence , biophysics , transporter , ctd , crystallography , membrane , biochemistry , amino acid , biology , peptidoglycan , enzyme , gene , receptor , oceanography , geology
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 β‐sheet and an outer shell of α‐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. Proteins 2016; 84:1328–1332. © 2016 Wiley Periodicals, Inc.