Journal
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Volume 84, Issue 9, Pages 1321-1327Publisher
WILEY
DOI: 10.1002/prot.25070
Keywords
protease; hyperthermophilic archaea; Ni binding; substrate recognition; C-terminal cleavage
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Funding
- Ministry of Education, Culture, Sports, Science, and Technology of Japan [26291012]
- Grants-in-Aid for Scientific Research [26291012] Funding Source: KAKEN
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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 angstrom resolution to better understand this process. TkHybD exhibits an // 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. (c) 2016 Wiley Periodicals, Inc.
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