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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >X-ray structure of the first 'extremo-α-carbonic anhydrase', a dimeric enzyme from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1
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X-ray structure of the first 'extremo-α-carbonic anhydrase', a dimeric enzyme from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1

机译：x射线结构第一extremo -α碳酸脱水酶”,的二聚的酶嗜热细菌Sulfurihydrogenibiumyellowstonense YO3AOP1

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摘要

SspCA, a novel 'extremo-α-carbonic anhydrase' isolated from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1, is an efficient catalyst for the hydration of CO2 and presents exceptional thermostability. Indeed, SspCA retains a high catalytic activity even after being heated to 343-373 14;K for several hours. Here, the crystallographic structure of this α-carbonic anhydrase (α-CA) is reported and the factors responsible for its function at high temperature are elucidated. In particular, the study suggests that increased structural compactness, together with an increased number of charged residues on the protein surface and a greater number of ionic networks, seem to be the key factors involved in the higher thermostability of this enzyme with respect to its mesophilic homologues. These findings are of extreme importance, since they provide a structural basis for the understanding of the mechanisms responsible for thermal stability in the α-CA family for the first time. The data obtained offer a tool that can be exploited to engineer α-CAs in order to obtain enzymes with enhanced thermostability for use in the harsh conditions of the CO2 capture and sequestration processes.
机译：SspCA,小说extremo -α碳酸脱水酶的从嗜热细菌隔离Sulfurihydrogenibium yellowstonense YO3AOP1,一个高效的催化剂二氧化碳的水合作用优异的热稳定性和礼物。甚至SspCA保持较高的催化活性在被加热到343 - 373年14;K数个小时。这α碳酸脱水酶(αca)和报道负责其功能在高的因素温度是阐明。研究表明,增加结构密实度,连同增加的数量蛋白质表面的残留物和指控更多的离子网络,似乎越高的关键因素这种酶的热稳定性对嗜中温同系物。极端的重要性,因为它们提供一个结构的理解的基础负责热稳定性机制家庭第一次α的ca。提供一个工具,可以利用获得的工程师αcas为了获得酶提高耐热性在严酷的使用二氧化碳捕集与封存条件流程。

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