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首页> 外文期刊>Biochemistry >The βγ-Crystallin Superfamily Contains a Universal Motif for Binding Calcium†,‡
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The βγ-Crystallin Superfamily Contains a Universal Motif for Binding Calcium†,‡

机译：βγ-晶体蛋白超家族包含一个与钙结合的通用基序†，‡

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The βγ-crystallin superfamily consists of evolutionarily related proteins with domain topologynsimilar to lens β- and γ-crystallins, formed from duplicatedGreek key motifs. Ca2þnbinding was found in a fewnβγ-crystallin members earlier, although its prevalence and diversity as inherent molecular properties amongnmembers of the superfamily are not well studied. To increase our understanding of Ca2þnbinding in variousnβγ-crystallins, we undertook comprehensive structural and Ca2þn-binding studies of seven members of thensuperfamily from bacteria, archaea, and vertebrates, including determination of high-resolution crystalnstructures of three proteins. Our structural observations show that the determinants of Ca2þncoordinationnremain conserved in the form of an N/D-N/D-#-I-S/T-S motif in all domains. However, binding of Ca2þnelicits varied physicochemical responses, ranging from passive sequestration to active stabilization. The motifnin this superfamily is modified in some members like lens crystallins where Ca2þn-binding abilities are partly orncompletely compromised. We show that reduction or loss of Ca2þnbinding in members of the superfamily,nparticularly in vertebrates, is due to the selective presence of unfavorable amino acids (largely Arg) at keynCa2þn-ligation positions and that engineering of the canonical Ca2þn-binding residues can confer bindingnactivity on an otherwise inactive domain. Through this work, we demonstrate that βγ-crystallins with the ND-N/D-#-I-S/T-S motif form an extensive set of Ca2þn-binding proteins prevalent in all of the three kingdomsnof life.
机译：βγ-晶状体蛋白超家族由具有与晶状体β-和γ-晶状体蛋白相似的结构域拓扑结构的进化相关蛋白组成，由重复的希腊关键基序形成。 Ca2þn结合较早地出现在少数几个βγ-晶状蛋白成员中，尽管对它的普遍性和多样性作为超家族成员中固有的分子性质的研究还不够。为了增进我们对各种βγ-晶状体蛋白中Ca 2+结合的了解，我们对细菌，古细菌和脊椎动物的当时超家族的七个成员进行了全面的结构和Ca 2n结合研究，包括测定三种蛋白质的高分辨率晶体结构。我们的结构观察表明，在所有域中，Ca2 +协调性的决定因素均以N / D-N / D-＃-I-S / T-S主题的形式保留。但是，钙离子结合会改变物理化学反应，从被动螯合到主动稳定。这个超家族的基序在某些成员中得到了修饰，例如晶状体晶状体，其中Ca2þn结合能力被部分或完全破坏。我们表明，减少或丢失的超家族成员，特别是在脊椎动物中的Ca2þnbinding是由于在keynCa2þn-连接位置选择性存在不利的氨基酸（主要是Arg）和规范的Ca2þn结合残基的工程可以赋予结合活性在原本不活跃的域上。通过这项工作，我们证明具有N / nD-N / D-＃-I-S / T-S模体的βγ-晶状蛋白形成了广泛的Ca2n-结合蛋白集，这些蛋白普遍存在于整个生命的三个王国中。

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