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 : 2023-09-09 DOI:10.1101/2022.12.25.521900

Mehmet Gul, Busra Yuksel, H. Bulut, H. Demirci

引用次数: 0

Abstract

Candida boidinii NAD+-dependent formate dehydrogenase (CbFDH) has gained significant attention for its potential applications in the production of biofuels and various industrial chemicals from inorganic carbon dioxide. The present study reports the atomic X-ray crystal structures of the wild-type CbFDH at cryogenic and ambient temperatures as well as 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 mutant CbFDH’s active site, 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, our 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突变型假丝酵母甲酸脱氢酶的x射线晶体学结构分析

假丝酵母(Candida boidinii) 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受到广泛关注。本研究报道了野生型CbFDH在低温和环境温度下的原子x射线晶体结构，以及在土耳其光源“土耳其软糖”下测定的低温下Val120Thr突变体。这些结构揭示了突变体CbFDH活性位点的Thr120和水分子之间新的氢键，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验证这些假设。总的来说，我们的发现为未来的蛋白质工程工作提供了宝贵的见解，这些工作可能会提高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.