Ontology highlight
ABSTRACT:
SUBMITTER: Mavrici D
PROVIDER: S-EPMC4050617 | biostudies-literature | 2014 Jun
REPOSITORIES: biostudies-literature
Mavrici Daniela D Marakalala Mohlopheni J MJ Holton James M JM Prigozhin Daniil M DM Gee Christine L CL Zhang Yanjia J YJ Rubin Eric J EJ Alber Tom T
Proceedings of the National Academy of Sciences of the United States of America 20140519 22
Bacterial growth and cell division are coordinated with hydrolysis of the peptidoglycan (PG) layer of the cell wall, but the mechanisms of regulation of extracellular PG hydrolases are not well understood. Here we report the biochemical, structural, and genetic analysis of the Mycobacterium tuberculosis homolog of the transmembrane PG-hydrolase regulator, FtsX. The purified FtsX extracellular domain binds the PG peptidase Rv2190c/RipC N-terminal segment, causing a conformational change that acti ...[more]