Autor: |
Jawaher Alenazi, Stephen Mayclin, Sandhya Subramanian, Peter J. Myler, Oluwatoyin A. Asojo |
Rok vydání: |
2022 |
Předmět: |
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Zdroj: |
Acta Crystallographica Section F Structural Biology Communications. 78:52-58 |
ISSN: |
2053-230X |
Popis: |
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. |
Databáze: |
OpenAIRE |
Externí odkaz: |
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