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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Analysis of protein solvent interactions in glucose dehydrogenase from the extreme halophile Haloferax mediterranei
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Analysis of protein solvent interactions in glucose dehydrogenase from the extreme halophile Haloferax mediterranei

机译：极端嗜盐菌Haloferax mediterranei的葡萄糖脱氢酶中蛋白质溶剂相互作用的分析

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摘要

The structure of glucose dehydrogenase from the extreme halophile Haloferax mediterranei has been solved at 1.6-angstrom resolution under crystallization conditions which closely mimic the "in vivo" intracellular environment. The decoration of the enzyme's surface with acidic residues is only partially neutralized by bound potassium counterions, which also appear to play a role in substrate binding. The surface shows the expected reduction in hydrophobic character, surprisingly not from changes associated with the loss of exposed hydrophobic residues but rather arising from a loss of lysines consistent with the genome wide-reduction of this residue in extreme halophiles. The structure reveals a highly ordered, multilayered solvation shell that can be seen to be organized into one dominant network covering much of the exposed surface accessible area to an extent not seen in almost any other protein structure solved. This finding is consistent with the requirement of the enzyme to form a protective shell in a dehydrating environment.
机译：来自极端嗜盐菌Haloferax mediterranei的葡萄糖脱氢酶的结构已经在接近模拟“体内”细胞内环境的结晶条件下以1.6埃的分辨率被解析。带有酸性残基的酶表面装饰仅被结合的钾抗衡离子部分中和，钾的抗衡离子也似乎在底物结合中起作用。该表面显示出预期的疏水特性降低，这出乎意料地不是由于与暴露的疏水残基丢失有关的变化，而是由赖氨酸的丢失引起的，该变化与极端嗜盐菌中该残基的基因组广泛减少相一致。该结构揭示了一个高度有序的多层溶剂化壳，可以看到它组织成一个占主导地位的网络，覆盖了大部分暴露的表面可及区域，其程度几乎是所解决的任何其他蛋白质结构所没有的。这一发现与酶在脱水环境中形成保护壳的要求是一致的。

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