Novel Β-structure of YLR301w from Saccharomyces cerevisiae

KimK.-H.; AhnH.J.; LeeW.-K.LeeC.YuM.-H.KimE.E.

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Novel Β-structure of YLR301w from Saccharomyces cerevisiae

机译：小说ΒYLR301w从酿酒的结构酵母

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When the Z-type variant of human 1-antitrypsin was overexpressed in Saccharomyces cerevisiae, proteomics analysis identified YLR301w as one of the up-regulated proteins. YLR301w is a 27.5 kDa protein with no sequence homology to any known protein and has been reported to interact with Sec72 and Hrr25. The crystal structure of S. cerevisiae YLR301w has been determined at 2.3 ? resolution, revealing a novel Β-structure. It consists of an N - terminal ten-stranded Β-barrel with two short -helices connected by a 23-residue linker to a seven-stranded half-barrel with two short helices at the C-terminus. The N - terminal barrel has a highly conserved hydrophobic channel that can bind hydrophobic molecules such as PEG. It forms a homodimer both in the crystal and in solution. YLR301w binds Sec72 with a K d of 6.2 μM, but the biological significance of this binding requires further investigation.

机译：当人类1-antitrypsin的z形变体在酿酒酵母,蛋白质组学分析确定YLR301w之一差异蛋白质。蛋白质,没有任何已知的序列同源性蛋白质和报道与Sec72 Hrr25。酵母YLR301w已经确定在2.3吗?分辨率,揭示小说Β结构。由一个N -末端ten-strandedΒ桶有两个短螺旋由23-residue连接链接到一个seven-stranded half-barrel有两个在糖基短螺旋。桶有一个高度保守的疏水通道可以绑定挂钩等疏水性分子。它形成为在水晶和解决方案。μM,但它的生物学意义绑定需要进一步调查。

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《Acta crystallographica.Section D. Biological crystallography》 |2012年第5期|531-540|共10页
作者
KimK.-H.; AhnH.J.; LeeW.-K.LeeC.YuM.-H.KimE.E.;
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作者单位

Biomedical Research Institute, Korea Institute of Science and Technology, 39-1 Hawolkok-dong;

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正文语种英语
中图分类化学;
关键词
Saccharomyces cerevisiae; homodimer; Homologous Sequencesβ-Barrel;

机译：酿酒酵母;为同源序列β桶;

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Novel Β-structure of YLR301w from Saccharomyces cerevisiae

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