Proteins Structure Function and Bioinformatics · 2016 · 15 citations · 24 references
Life SciencesBiochemistryMicrobiologyEnzyme MechanismEnzymologyStructural BiologyCatalytic MechanismsEnzyme FunctionEnzyme-substrate RecognitionProtein StructureStructural EnzymologyThermostable EnzymesActive Site Metal BindingBacterial ProteasesBinding Site PredictionCrystal Structure PredictionNickel Enzymes
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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Clustal W and Clustal X version 2.0
Mark Larkin, Gordon Blackshields, Nigel P. Brown et al. · Bioinformatics · 2007 · 29.1K citations · Full text
<i>Phaser</i>crystallographic software
Airlie J. McCoy, Ralf W. Grosse‐Kunstleve, Paul D. Adams et al. · Journal of Applied Crystallography · 2007 · 20.9K citations · Full text