Ontology highlight
ABSTRACT:
SUBMITTER: Bridwell-Rabb J
PROVIDER: S-EPMC5137760 | biostudies-literature | 2016 Nov
REPOSITORIES: biostudies-literature
Bridwell-Rabb Jennifer J Kang Gyunghoon G Zhong Aoshu A Liu Hung-Wen HW Drennan Catherine L CL
Proceedings of the National Academy of Sciences of the United States of America 20161114 48
HD domain phosphohydrolase enzymes are characterized by a conserved set of histidine and aspartate residues that coordinate an active site metallocenter. Despite the important roles these enzymes play in nucleotide metabolism and signal transduction, few have been both biochemically and structurally characterized. Here, we present X-ray crystal structures and biochemical characterization of the Bacillus megaterium HD domain phosphohydrolase OxsA, involved in the biosynthesis of the antitumor, an ...[more]