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

IF 2.6 4区生物学 Q2 BIOCHEMICAL RESEARCH METHODS

Acta Crystallographica. Section D, Structural Biology Pub Date : 2023-11-01 Epub Date: 2023-10-20 DOI:10.1107/S2059798323008070

Mehmet Gul, Busra Yuksel, Huri Bulut, Hasan DeMirci

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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.

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野生型和Val120Thr突变型博伊迪尼念珠菌甲酸脱氢酶的X射线晶体学结构分析。

布氏假丝酵母NAD+依赖性甲酸脱氢酶（CbFDH）因其在利用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。本研究报道了在土耳其光源“Turkish DeLight”测定的野生型CbFDH在低温和环境温度下的原子X射线晶体结构，以及Val120Thr突变体在低温下的原子X-射线晶体结构。这些结构揭示了突变体CbFDH活性位点中Thr120和水分子之间的新氢键，表明活性位点的稳定性增加，反应过程中电子转移更有效。需要进一步的实验数据来检验这些假设。总之，这些发现为未来的蛋白质工程工作提供了宝贵的见解，有可能提高CbFDH的效率和有效性。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Acta Crystallographica. Section D, Structural Biology BIOCHEMICAL RESEARCH METHODSBIOCHEMISTRY &-BIOCHEMISTRY & MOLECULAR BIOLOGY

CiteScore

4.50

自引率

13.60%

发文量

216

期刊介绍： Acta Crystallographica Section D welcomes the submission of articles covering any aspect of structural biology, with a particular emphasis on the structures of biological macromolecules or the methods used to determine them. Reports on new structures of biological importance may address the smallest macromolecules to the largest complex molecular machines. These structures may have been determined using any structural biology technique including crystallography, NMR, cryoEM and/or other techniques. The key criterion is that such articles must present significant new insights into biological, chemical or medical sciences. The inclusion of complementary data that support the conclusions drawn from the structural studies (such as binding studies, mass spectrometry, enzyme assays, or analysis of mutants or other modified forms of biological macromolecule) is encouraged. Methods articles may include new approaches to any aspect of biological structure determination or structure analysis but will only be accepted where they focus on new methods that are demonstrated to be of general applicability and importance to structural biology. Articles describing particularly difficult problems in structural biology are also welcomed, if the analysis would provide useful insights to others facing similar problems.