Crystal structure of a short-chain dehydrogenase/reductase from Burkholderia phymatum in complex with NAD.

ABSTRACT: Burkholderia phymatum is an important symbiotic nitrogen-fixing betaproteobacterium. B. phymatum is beneficial, unlike other Burkholderia species, which cause disease or are potential bioagents. Structural genomics studies at the SSGCID include characterization of the structures of short-chain dehydrogenases/reductases (SDRs) from multiple Burkholderia species. The crystal structure of a short-chain dehydrogenase from B. phymatum (BpSDR) was determined in space group C222₁ at a resolution of 1.80 Å. BpSDR shares less than 38% sequence identity with any known structure. The monomer is a prototypical SDR with a well conserved cofactor-binding domain despite its low sequence identity. The substrate-binding cavity is unique and offers insights into possible functions and likely inhi

SUBMITTER: Alenazi J 

PROVIDER: S-EPMC8805215 | biostudies-literature | 2022 Feb

REPOSITORIES: biostudies-literature