Ontology highlight
ABSTRACT:
SUBMITTER: Mittelstadt G
PROVIDER: S-EPMC4972205 | biostudies-literature | 2016 Aug
REPOSITORIES: biostudies-literature
Mittelstädt Gerd G Moggré Gert-Jan GJ Panjikar Santosh S Nazmi Ali Reza AR Parker Emily J EJ
Protein science : a publication of the Protein Society 20160606 8
Adenosine triphosphate phosphoribosyltransferase (ATP-PRT) catalyzes the first committed step of the histidine biosynthesis in plants and microorganisms. Here, we present the functional and structural characterization of the ATP-PRT from the pathogenic ε-proteobacteria Campylobacter jejuni (CjeATP-PRT). This enzyme is a member of the long form (HisGL ) ATP-PRT and is allosterically inhibited by histidine, which binds to a remote regulatory domain, and competitively inhibited by AMP. In the cryst ...[more]