SH3‐like motif‐containing C‐terminal domain of staphylococcal teichoic acid transporter suggests possible function |
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| Authors: | Tzu‐Ping Ko Shih‐Ting Tseng Shu‐Jung Lai Sheng‐Chia Chen Hong‐Hsiang Guan Chia Shin Yang Chun Jung Chen Yeh Chen |
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| Affiliation: | 1. Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan;2. Department of Food and Nutrition, Providence University, Taichung City, Taiwan;3. Department of Endocrinology and Metabolism, Kuang Tien General Hospital, Taiwan;4. Department of Biotechnology, Hungkuang University, Taichung, Taiwan;5. Life Science Group, Scientific Research Division, National Synchrotron Radiation Research Center, Hsinchu, Taiwan;6. Taiwan Advance Biopharm (TABP) Inc, Xizhi City, New Taipei City, Taiwan;7. Institute of Biotechnology and Center for Bioscience and Biotechnology, National Cheng Kung University, Tainan City, Taiwan;8. Department of Physics, National Tsing Hua University, Hsinchu, Taiwan |
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| 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. |
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| Keywords: | ABC transporter TagH WTA bacterial cell wall crystal structure |
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