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Crystal structure of a [NiFe] hydrogenase maturation protease HybD from Thermococcus kodakarensis KOD1
Authors:Sunghark Kwon  Yuichi Nishitani  Satoshi Watanabe  Yoshinori Hirao  Tadayuki Imanaka  Tamotsu Kanai  Haruyuki Atomi  Kunio Miki
Institution:1. Department of Chemistry, Graduate School of Science, Kyoto University, Kyoto, Japan;2. Institute of Multidisciplinary Research for Advanced Materials, Tohoku University, Sendai, Japan;3. Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Kyoto, Japan;4. Research Organization of Science and Technology, Ritsumeikan University, Kusatsu, Japan;5. Japan Science and Technology Agency, CREST, Tokyo, Japan
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.
Keywords:protease  hyperthermophilic archaea  Ni binding  substrate recognition  C‐terminal cleavage
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