Ontology highlight
ABSTRACT:
SUBMITTER: Whitehouse S
PROVIDER: S-EPMC3518217 | biostudies-literature | 2012 Dec
REPOSITORIES: biostudies-literature
Whitehouse Sarah S Gold Vicki A M VA Robson Alice A Allen William J WJ Sessions Richard B RB Collinson Ian I
The Journal of cell biology 20121203 6
The bacterial ATPase SecA and protein channel complex SecYEG form the core of an essential protein translocation machinery. The nature of the conformational changes induced by each stage of the hydrolytic cycle of ATP and how they are coupled to protein translocation are not well understood. The structure of the SecA-SecYEG complex revealed a 2-helix-finger (2HF) of SecA in an ideal position to contact the substrate protein and push it through the membrane. Surprisingly, immobilization of this f ...[more]