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首页> 外文期刊>Journal of Molecular Biology >Evolution of structure and function in the o-succinylbenzoate synthase/N-acylamino acid racemase family of the enolase superfamily
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Evolution of structure and function in the o-succinylbenzoate synthase/N-acylamino acid racemase family of the enolase superfamily

机译：烯醇化酶超家族的邻-琥珀酰苯甲酸酯合酶/ N-酰基氨基酸消旋酶家族的结构和功能的演变

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摘要

Understanding how proteins evolve to provide both exquisite specificity and proficient activity is a fundamental problem in biology that has implications for protein function prediction and protein engineering. To study this problem, we analyzed the evolution of structure and function in the o-succinylbenzoate synthase/N-acylamino acid racemase (OSBS/NAAAR) family, part of the mechanistically diverse enolase superfamily. Although all characterized members of the family catalyze the OSBS reaction, this family is extraordinarily divergent, with some members sharing < 15% identity. In addition, a member of this family, Amycolatopsis OSBS/NAAAR, is promiscuous, catalyzing both dehydration and racemization. Although the OSBS/NAAAR family appears to have a single evolutionary origin, no sequence or structural motifs unique to this family could be identified; all residues conserved in the family are also found in enolase superfamily members that have different functions. Based on their species distribution, several uncharacterized proteins similar to Amycolatopsis OSBS/NAAAR appear to have been transmitted by lateral gene transfer. Like Amycolatopsis OSBS/NAAAR, these might have additional or alternative functions to OSBS because many are from organisms lacking the pathway in which OSBS is an intermediate. In addition to functional differences, the OSBS/NAAAR family exhibits surprising structural variations, including large differences in orientation between the two domains. These results offer several insights into protein evolution. First, orthologous proteins can exhibit significant structural variation, and specificity can be maintained with little conservation of ligand-contacting residues. Second, the discovery of a set of proteins similar to Amycolatopsis OSBS/NAAAR supports the hypothesis that new protein functions evolve through promiscuous intermediates. Finally, a combination of evolutionary, structural, and sequence analyses identified characteristics that might prime proteins, such as Amycolatopsis OSBS/NAAAR, for the evolution of new activities. (c) 2006 Elsevier Ltd. All rights reserved.
机译：了解蛋白质如何进化以提供出色的特异性和熟练的活性是生物学中的一个基本问题，对蛋白质功能预测和蛋白质工程具有影响。为了研究此问题，我们分析了邻-琥珀酰苯甲酸酯合酶/ N-酰基氨基酸消旋酶（OSBS / NAAAR）家族的结构和功能的演变，该家族是机制多样的烯醇酶超家族的一部分。尽管该家族中所有有特征的成员都催化OSBS反应，但该家族的分歧非常大，有些成员的认同度低于15％。此外，该家族的成员，淀粉样变性OSBS / NAAAR混杂，催化脱水和消旋。尽管OSBS / NAAAR家族似乎具有单一的进化起源，但无法鉴定出该家族独有的序列或结构基序。在具有不同功能的烯醇化酶超家族成员中也发现了该家族中所有保守的残基。根据它们的种类分布，一些未表征的蛋白类似于支原体OSBS / NAAAR，似乎是通过侧向基因转移而传播的。像真菌病OSBS / NAAAR一样，它们可能具有OSBS的附加或替代功能，因为许多来自缺乏OSBS中间途径的生物。除了功能差异外，OSBS / NAAAR系列还表现出令人惊讶的结构变化，包括两个结构域之间的方向差异很大。这些结果为蛋白质进化提供了一些见识。首先，直系同源蛋白可以表现出显着的结构变异，并且可以在几乎不保留配体接触残基的情况下保持特异性。其次，发现了一组类似于支原体OSBS / NAAAR的蛋白质，这支持了新蛋白质功能通过混杂中间体进化的假设。最终，将进化，结构和序列分析相结合，确定了可能引发蛋白质（例如支链淀粉OSBS / NAAAR）用于新活性进化的特征。 （c）2006 Elsevier Ltd.保留所有权利。

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