Crystal structure of a [NiFe] hydrogenase maturation protease HybD from  Thermococcus kodakarensis  KOD1 | Zendy

Kwon Sunghark | Zendy; Nishitani Yuichi | Zendy; Watanabe Satoshi | Zendy; Hirao Yoshinori | Zendy; Imanaka Tadayuki | Zendy; Kanai Tamotsu | Zendy; Atomi Haruyuki | Zendy; Miki Kunio | Zendy

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Crystal structure of a [NiFe] hydrogenase maturation protease HybD from Thermococcus kodakarensis KOD1

Author(s) -

Kwon Sunghark,

Nishitani Yuichi,

Watanabe Satoshi,

Hirao Yoshinori,

Imanaka Tadayuki,

Kanai Tamotsu,

Atomi Haruyuki,

Miki Kunio

Publication year - 2016

Publication title -

proteins: structure, function, and bioinformatics

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.699

H-Index - 191

eISSN - 1097-0134

pISSN - 0887-3585

DOI - 10.1002/prot.25070

Subject(s) - thermococcus , hydrogenase , protease , cleavage (geology) , biology , catalysis , chemistry , crystallography , biochemistry , archaea , enzyme , gene , paleontology , fracture (geology)

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.

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