Crystal structure of a short-chain dehydrogenase/reductase from Burkholderia phymatum in complex with NAD.
Crystal structure of a short-chain dehydrogenase/reductase from Burkholderia phymatum in complex with NAD.
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DOI：
10.1107/s2053230x22000218
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发表时间：
2022-02-01
期刊：
影响因子：
--
通讯作者：
Asojo OA
中科院分区：
文献类型：
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作者：
Alenazi J;Mayclin S;Subramanian S;Myler PJ;Asojo OA
植酸伯克霍尔德氏菌短链脱氢酶/还原酶的晶体结构为其可能的功能和酶功能的可能抑制剂提供了深入的了解。植酸伯克霍尔德氏菌是一种重要的共生固氮β-蛋白细菌。与其他伯克霍尔德氏菌不同，植酸杆菌是有益的，其他伯克霍尔德氏菌会引起疾病或成为潜在的生物制剂。SSGCID的结构基因组学研究包括对来自多种伯克霍尔德氏菌的短链脱氢酶/还原酶(SDR)的结构进行表征。在C2221空间群中测定了植酸杆菌短链脱氢酶(BpSDR)的晶体结构，其分辨率为1.80 ä。BpSDR与任何已知结构的序列同源性都不到38%。该单体是一个典型的SDR，具有保守的辅因子结合域，尽管其序列同源性较低。底物结合腔是独一无二的，它提供了对BpSDR可能的功能和可能的酶功能抑制剂的见解。
The crystal structure of a short-chain dehydrogenase/reductase from Burkholderia phymatum offers insights into its possible functions and likely inhibitors of its enzymatic functions. 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.