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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >A novel interdomain interface in crystallins: Structural characterization of the βγ-crystallin from Geodia cydonium at 0.99 14;? resolution
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A novel interdomain interface in crystallins: Structural characterization of the βγ-crystallin from Geodia cydonium at 0.99 14;? resolution

机译：小说在晶状体蛋白interdomain接口:结构表征的βγ晶状体蛋白在0.99 14;从Geodia cydonium吗?

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摘要

The βγ-crystallin superfamily includes highly diverse proteins belonging to all of the kingdoms of life. Based on structural topology, these proteins are considered to be evolutionarily related to the long-lived βγ-crystallins that constitute the vertebrate eye lens. This study reports the crystallographic structure at 0.99 14;? resolution of the two-domain βγ-crystallin (geodin) from the sponge Geodia cydonium. This is the most ancient member of the βγ-crystallin superfamily in metazoans. The X-ray structure shows that the geodin domains adopt the typical βγ-crystallin fold with a paired Greek-key motif, thus confirming the hypothesis that the crystallin-type scaffold used in the evolution of bacteria and moulds was recruited very early in metazoans. As a significant new structural feature, the sponge protein possesses a unique interdomain interface made up by pairing between the second motif of the first domain and the first motif of the second domain. The atomic resolution also allowed a detailed analysis of the calcium-binding site of the protein.
机译：的βγ晶状体蛋白总科包括高度不同的蛋白质属于所有的王国的生活。蛋白质被认为是进化有关长寿的βγ-crystallins构成脊椎动物眼睛的镜头。报告在0.99的晶体结构14; ?(geodin)海绵Geodia cydonium。最古老的成员βγ晶状体蛋白在后生动物总科。表明geodin领域采用的典型βγ晶状体蛋白折叠Greek-key图案配对,从而确认的假说crystallin-type支架用于的进化细菌和霉菌是招募非常早后生动物。海绵特性,具有一种独特的蛋白质interdomain接口由之间的配对第二主题的第一个域和第二个领域的第一主题。决议还允许一个详细的分析的钙结合的蛋白质。

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