Premium
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)
ABSTRACT 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.