Ontology highlight
ABSTRACT:
SUBMITTER: Smirnova I
PROVIDER: S-EPMC4653160 | biostudies-literature | 2015 Nov
REPOSITORIES: biostudies-literature
Smirnova Irina I Kasho Vladimir V Jiang Xiaoxu X Pardon Els E Steyaert Jan J Kaback H Ronald HR
Proceedings of the National Academy of Sciences of the United States of America 20151028 45
The lactose permease of Escherichia coli (LacY), a highly dynamic membrane protein, catalyzes symport of a galactopyranoside and an H(+) by using an alternating access mechanism, and the transport cycle involves multiple conformational states. Single-domain camelid nanobodies (Nbs) developed against a LacY mutant immobilized in an outward (periplasmic)-open conformation bind to the flexible WT protein and stabilize the open-outward conformation(s). Here, we use site-directed, distance-dependent ...[more]