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X 射线晶体学分析野生型和 Val120Thr 突变型毕赤酵母甲酸脱氢酶的结构。

Structural analysis of wild-type and Val120Thr mutant Candida boidinii formate dehydrogenase by X-ray crystallography.

机构信息

Department of Molecular Biology and Genetics, Koc University, 34450 Istanbul, Türkiye.

Department of Medical Biochemistry, Faculty of Medicine, Istinye University, 34010 Istanbul, Türkiye.

出版信息

Acta Crystallogr D Struct Biol. 2023 Nov 1;79(Pt 11):1010-1017. doi: 10.1107/S2059798323008070. Epub 2023 Oct 20.

Abstract

Candida boidinii NAD-dependent formate dehydrogenase (CbFDH) has gained significant attention for its potential application in the production of biofuels and various industrial chemicals from inorganic carbon dioxide. The present study reports the atomic X-ray crystal structures of wild-type CbFDH at cryogenic and ambient temperatures, as well as that of the Val120Thr mutant at cryogenic temperature, determined at the Turkish Light Source `Turkish DeLight'. The structures reveal new hydrogen bonds between Thr120 and water molecules in the active site of the mutant CbFDH, suggesting increased stability of the active site and more efficient electron transfer during the reaction. Further experimental data is needed to test these hypotheses. Collectively, these findings provide invaluable insights into future protein-engineering efforts that could potentially enhance the efficiency and effectiveness of CbFDH.

摘要

博伊丁假丝酵母烟酰胺腺嘌呤二核苷酸(NAD)依赖型甲酸盐脱氢酶(CbFDH)因其在从无机二氧化碳生产生物燃料和各种工业化学品方面的潜在应用而备受关注。本研究报告了野生型 CbFDH 在低温和常温下的原子 X 射线晶体结构,以及在土耳其光源“Turkish DeLight”下低温下 Val120Thr 突变体的原子 X 射线晶体结构。这些结构揭示了突变型 CbFDH 活性位点中 Thr120 与水分子之间的新氢键,表明活性位点的稳定性增加,反应过程中的电子转移更有效。需要进一步的实验数据来验证这些假设。总的来说,这些发现为未来的蛋白质工程研究提供了宝贵的见解,这可能会提高 CbFDH 的效率和效果。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fa09/10619422/b23be8197154/d-79-01010-fig1.jpg

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