Ontology highlight
ABSTRACT:
SUBMITTER: Kumazaki K
PROVIDER: S-EPMC4252904 | biostudies-literature | 2014
REPOSITORIES: biostudies-literature
Kumazaki Kaoru K Kishimoto Toshiki T Furukawa Arata A Mori Hiroyuki H Tanaka Yoshiki Y Dohmae Naoshi N Ishitani Ryuichiro R Tsukazaki Tomoya T Nureki Osamu O
Scientific reports 20141203
Bacterial YidC, an evolutionally conserved membrane protein, functions as a membrane protein chaperone in cooperation with the Sec translocon and as an independent insertase for membrane proteins. In Gram-negative bacteria, the transmembrane and periplasmic regions of YidC interact with the Sec proteins, forming a multi-protein complex for Sec-dependent membrane protein integration. Here, we report the crystal structure of full-length Escherichia coli YidC. The structure reveals that a hydrophil ...[more]