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

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 inhibitors of the enzymatic functions of BpSDR.
Source: Acta Crystallographica Section F - Category: Biochemistry Authors: Tags: SSGCID oxidoreductases Burkholderia phymatum short-chain dehydrogenase/reductase family NAD structural genomics Seattle Structural Genomics Center for Infectious Disease research communications Source Type: research