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

Autor:	Jawaher Alenazi, Stephen Mayclin, Sandhya Subramanian, Peter J. Myler, Oluwatoyin A. Asojo
Rok vydání:	2022
Předmět:	Models Molecular Binding Sites Burkholderiaceae Protein Conformation Coenzymes Biophysics Crystallography X-Ray NAD Condensed Matter Physics Biochemistry Short Chain Dehydrogenase-Reductases Bacterial Proteins Structural Biology Genetics
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:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::92e220dc6bf854a75cdd7f26960a25ef https://doi.org/10.1107/s2053230x22000218 Zobrazit plný text záznamu Plný text ve formátu PDF Plný text ve formátu HTML
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