Ontology highlight
ABSTRACT:
SUBMITTER: Cao Y
PROVIDER: S-EPMC3077569 | biostudies-literature | 2011 Mar
REPOSITORIES: biostudies-literature
Cao Yu Y Jin Xiangshu X Huang Hua H Derebe Mehabaw Getahun MG Levin Elena J EJ Kabaleeswaran Venkataraman V Pan Yaping Y Punta Marco M Love James J Weng Jun J Quick Matthias M Ye Sheng S Kloss Brian B Bruni Renato R Martinez-Hackert Erik E Hendrickson Wayne A WA Rost Burkhard B Javitch Jonathan A JA Rajashankar Kanagalaghatta R KR Jiang Youxing Y Zhou Ming M
Nature 20110213 7338
The TrkH/TrkG/KtrB proteins mediate K(+) uptake in bacteria and probably evolved from simple K(+) channels by multiple gene duplications or fusions. Here we present the crystal structure of a TrkH from Vibrio parahaemolyticus. TrkH is a homodimer, and each protomer contains an ion permeation pathway. A selectivity filter, similar in architecture to those of K(+) channels but significantly shorter, is lined by backbone and side-chain oxygen atoms. Functional studies showed that TrkH is selective ...[more]