Ontology highlight
ABSTRACT:
SUBMITTER: Stogios PJ
PROVIDER: S-EPMC4844700 | biostudies-literature | 2016 Apr
REPOSITORIES: biostudies-literature
Stogios Peter J PJ Cox Georgina G Spanogiannopoulos Peter P Pillon Monica C MC Waglechner Nicholas N Skarina Tatiana T Koteva Kalinka K Guarné Alba A Savchenko Alexei A Wright Gerard D GD
Nature communications 20160422
Rifampin (RIF) phosphotransferase (RPH) confers antibiotic resistance by conversion of RIF and ATP, to inactive phospho-RIF, AMP and Pi. Here we present the crystal structure of RPH from Listeria monocytogenes (RPH-Lm), which reveals that the enzyme is comprised of three domains: two substrate-binding domains (ATP-grasp and RIF-binding domains); and a smaller phosphate-carrying His swivel domain. Using solution small-angle X-ray scattering and mutagenesis, we reveal a mechanism where the swivel ...[more]