Crystal structure of a putative short-chain dehydrogenase/reductase from Paraburkholderia xenovorans.
Crystal structure of a putative short-chain dehydrogenase/reductase from Paraburkholderia xenovorans.
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DOI：
10.1107/s2053230x21012632
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发表时间：
2022-01-01
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：
Davidson J;Nicholas K;Young J;Conrady DG;Mayclin S;Subramanian S;Staker BL;Myler PJ;Asojo OA
高分辨率结构的推定短链还原酶从商业上重要的细菌Paraburkholderia xenovorans的报道。P. xenovorans降解有机废物，如多氯联苯。 Paraburkholderia xenovorans降解有机废物，包括多氯联苯。在空间群P21中以1.45 μ m的分辨率确定了来自P. xenovorans（PxSDR）的推定脱氢酶/还原酶（SDR）的原子结构。 PxSDR与任何已知的结构共享小于37%的序列同一性，并组装为原型SDR四聚体。正如预期的那样，在底物结合腔中存在一些构象灵活性和差异，这解释了底物特异性。独特的是，PxSDR的辅因子结合腔不是很保守，与其他SDR不同。PxSDR具有额外的七个氨基酸，其在辅因子结合腔中形成额外的独特环。需要进一步的研究来确定这些差异如何影响SDR的酶功能。
The high-resolution structure of a putative short-chain reductase from the commercially important bacterium Paraburkholderia xenovorans is reported. P. xenovorans degrades organic wastes such as polychlorinated biphenyls. Paraburkholderia xenovorans degrades organic wastes, including polychlorinated biphenyls. The atomic structure of a putative dehydrogenase/reductase (SDR) from P. xenovorans (PxSDR) was determined in space group P21 at a resolution of 1.45 Å. PxSDR shares less than 37% sequence identity with any known structure and assembles as a prototypical SDR tetramer. As expected, there is some conformational flexibility and difference in the substrate-binding cavity, which explains the substrate specificity. Uniquely, the cofactor-binding cavity of PxSDR is not well conserved and differs from those of other SDRs. PxSDR has an additional seven amino acids that form an additional unique loop within the cofactor-binding cavity. Further studies are required to determine how these differences affect the enzymatic functions of the SDR.