Ontology highlight
ABSTRACT:
SUBMITTER: Chiu HJ
PROVIDER: S-EPMC4188006 | biostudies-literature | 2014 Oct
REPOSITORIES: biostudies-literature
Chiu Hsiu Ju HJ Grant Joanna C JC Farr Carol L CL Jaroszewski Lukasz L Knuth Mark W MW Miller Mitchell D MD Elsliger Marc André MA Deacon Ashley M AM Godzik Adam A Lesley Scott A SA Wilson Ian A IA
Acta crystallographica. Section D, Biological crystallography 20140927 Pt 10
The crystal structure of arabinose-5-phosphate isomerase (API) from Bacteroides fragilis (bfAPI) was determined at 1.7 Å resolution and was found to be a tetramer of a single-domain sugar isomerase (SIS) with an endogenous ligand, CMP-Kdo (cytidine 5'-monophosphate-3-deoxy-D-manno-oct-2-ulosonate), bound at the active site. API catalyzes the reversible isomerization of D-ribulose 5-phosphate to D-arabinose 5-phosphate in the first step of the Kdo biosynthetic pathway. Interestingly, the bound CM ...[more]