Crystal structure of a [NiFe] hydrogenase maturation protease HybD from Thermococcus kodakarensis KOD1
Crystal structure of a [NiFe] hydrogenase maturation protease HybD from Thermococcus kodakarensis KOD1
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DOI：
10.1002/prot.25070
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发表时间：
2016-06
期刊：
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通讯作者：
Sunghark Kwon;Y. Nishitani;Satoshi Watanabe;Y. Hirao;T. Imanaka;T. Kanai;H. Atomi;K. Miki
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文献类型：
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作者：
Sunghark Kwon;Y. Nishitani;Satoshi Watanabe;Y. Hirao;T. Imanaka;T. Kanai;H. Atomi;K. Miki
来自 Thermococcus kodakarensis KOD1 (TkHybD) 的 [NiFe] 氢化酶成熟蛋白酶 HybD 参与通过 Ni 识别切割 [NiFe] 氢化酶大亚基的 C 末端残基。在这里，我们以 1.82 Å 的分辨率报告了 TkHybD 的晶体结构，以更好地理解这一过程。 TkHybD 表现出 α/β/α 夹心折叠，具有负责 Ni 识别的保守残基。 TkHybD 与同源蛋白的比较还表明它们具有共同的整体结构，表明它们具有相似的催化功能。我们的结果（包括金属结合位点预测）提供了对 TkHybD 底物识别和催化机制的深入了解。蛋白质 2016; 84：1321–1327。 © 2016 Wiley 期刊公司。
A [NiFe] hydrogenase maturation protease HybD from Thermococcus kodakarensis KOD1 (TkHybD) is involved in the cleavage of the C‐terminal residues of [NiFe] hydrogenase large subunits by Ni recognition. Here, we report the crystal structure of TkHybD at 1.82 Å resolution to better understand this process. TkHybD exhibits an α/β/α sandwich fold with conserved residues responsible for the Ni recognition. Comparisons of TkHybD with homologous proteins also reveal that they share a common overall architecture, suggesting that they have similar catalytic functions. Our results including metal binding site prediction provide insight into the substrate recognition and catalysis mechanism of TkHybD. Proteins 2016; 84:1321–1327. © 2016 Wiley Periodicals, Inc.