| Autor: |
Ko, Tzu‐Ping, Tseng, Shih‐Ting, Lai, Shu‐Jung, Chen, Sheng‐Chia, Guan, Hong‐Hsiang, Shin Yang, Chia, Jung Chen, Chun, Chen, Yeh |
| Zdroj: |
Proteins; Sep2016, Vol. 84 Issue 9, p1328-1332, 5p |
| Abstrakt: |
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 β-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. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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