Abstract
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.
Keywords:
ABC transporter; TagH; WTA; bacterial cell wall; crystal structure.
© 2016 Wiley Periodicals, Inc.
MeSH terms
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ATP-Binding Cassette Transporters / chemistry*
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ATP-Binding Cassette Transporters / genetics
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ATP-Binding Cassette Transporters / metabolism
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Amino Acid Motifs
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Bacterial Proteins / chemistry*
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism
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Binding Sites
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Biological Transport
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Cell Wall / chemistry
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Cloning, Molecular
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Crystallography, X-Ray
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Hydrolases / chemistry*
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Hydrolases / genetics
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Hydrolases / metabolism
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Models, Molecular
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Protein Binding
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Protein Interaction Domains and Motifs
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Protein Structure, Secondary
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Protein Subunits / chemistry*
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Protein Subunits / genetics
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Protein Subunits / metabolism
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Staphylococcus epidermidis / chemistry*
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Staphylococcus epidermidis / enzymology
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Static Electricity
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Teichoic Acids / chemistry*
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Teichoic Acids / metabolism
Substances
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ATP-Binding Cassette Transporters
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Bacterial Proteins
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Protein Subunits
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Recombinant Proteins
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Teichoic Acids
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Hydrolases