Ontology highlight
ABSTRACT:
SUBMITTER: Rivera-Cancel G
PROVIDER: S-EPMC4273353 | biostudies-literature | 2014 Dec
REPOSITORIES: biostudies-literature
Rivera-Cancel Giomar G Ko Wen-huang WH Tomchick Diana R DR Correa Fernando F Gardner Kevin H KH
Proceedings of the National Academy of Sciences of the United States of America 20141202 50
Although histidine kinases (HKs) are critical sensors of external stimuli in prokaryotes, the mechanisms by which their sensor domains control enzymatic activity remain unclear. Here, we report the full-length structure of a blue light-activated HK from Erythrobacter litoralis HTCC2594 (EL346) and the results of biochemical and biophysical studies that explain how it is activated by light. Contrary to the standard view that signaling occurs within HK dimers, EL346 functions as a monomer. Its str ...[more]