期刊
SCIENCE
卷 332, 期 6027, 页码 352-354出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1199098
关键词
-
资金
- Deutsche Forschungsgemeinschaft [Ei-520/3, An-676/1, IRTG 1478]
The formate transporter FocA was described to switch its mode of operation from a passive export channel at high external pH to a secondary active formate/H+ importer at low pH. The crystal structure of Salmonella typhimurium FocA at pH 4.0 shows that this switch involves a major rearrangement of the amino termini of individual protomers in the pentameric channel. The amino-terminal helices open or block transport in a concerted, cooperative action that indicates how FocA is gated in a pH-dependent way. Electrophysiological studies show that the protein acts as a specific formate channel at pH 7.0 and that it closes upon a shift of pH to 5.1.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据