Ontology highlight
ABSTRACT:
SUBMITTER: Kumar H
PROVIDER: S-EPMC4517220 | biostudies-literature | 2015 Jul
REPOSITORIES: biostudies-literature
Kumar Hemant H Kumar Hemant H Finer-Moore Janet S JS Kaback H Ronald HR Stroud Robert M RM
Proceedings of the National Academy of Sciences of the United States of America 20150708 29
The X-ray crystal structure of a conformationally constrained mutant of the Escherichia coli lactose permease (the LacY double-Trp mutant Gly-46→Trp/Gly-262→Trp) with bound p-nitrophenyl-α-d-galactopyranoside (α-NPG), a high-affinity lactose analog, is described. With the exception of Glu-126 (helix IV), side chains Trp-151 (helix V), Glu-269 (helix VIII), Arg-144 (helix V), His-322 (helix X), and Asn-272 (helix VIII) interact directly with the galactopyranosyl ring of α-NPG to provide specifici ...[more]