Structural highlights
Publication Abstract from PubMed
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 A resolution to better understand this process. TkHybD exhibits an alpha/beta/alpha 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. This article is protected by copyright. All rights reserved.
Crystal structure of a [NiFe] hydrogenase maturation protease HybD from Thermococcus kodakarensis KOD1.,Kwon S, Nishitani Y, Watanabe S, Hirao Y, Imanaka T, Kanai T, Atomi H, Miki K Proteins. 2016 May 18. doi: 10.1002/prot.25070. PMID:27192667[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kwon S, Nishitani Y, Watanabe S, Hirao Y, Imanaka T, Kanai T, Atomi H, Miki K. Crystal structure of a [NiFe] hydrogenase maturation protease HybD from Thermococcus kodakarensis KOD1. Proteins. 2016 May 18. doi: 10.1002/prot.25070. PMID:27192667 doi:http://dx.doi.org/10.1002/prot.25070
