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- Title
Crystal structure of a short‐chain dehydrogenase/reductase from Burkholderia phymatum in complex with NAD.
- Authors
Alenazi, Jawaher; Mayclin, Stephen; Subramanian, Sandhya; Myler, Peter J.; Asojo, Oluwatoyin A.
- 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 inhibitors of the enzymatic functions of BpSDR.
- Subjects
BURKHOLDERIA; CRYSTAL structure; DEHYDROGENASES; SPACE groups; REDUCTASES; GENOMICS
- Publication
Acta Crystallographica: Section F, Structural Biology Communications, 2022, Vol 78, Issue 2, p52
- ISSN
2053-230X
- Publication type
Article
- DOI
10.1107/S2053230X22000218