Ontology highlight
ABSTRACT:
SUBMITTER: Desai J
PROVIDER: S-EPMC5012948 | biostudies-literature | 2016 Sep
REPOSITORIES: biostudies-literature
Desai Janish J Liu Yi-Liang YL Wei Hongli H Liu Weidong W Ko Tzu-Ping TP Guo Rey-Ting RT Oldfield Eric E
ChemMedChem 20160726 17
We report the first structure of heptaprenyl diphosphate synthase from Staphylococcus aureus (SaHepPPS), together with an investigation of its mechanism of action and inhibition. The protein is involved in the formation of menaquinone, a key electron transporter in many bacteria, including pathogens. SaHepPPS consists of a "catalytic " subunit (SaHepPPS-2) having two "DDXXD" motifs and a "regulatory" subunit (SaHepPPS-1) that lacks these motifs. High concentrations of the substrates, isopentenyl ...[more]