2z1c
From Proteopedia
Crystal structure of HypC from Thermococcus kodakaraensis KOD1
Overview
[NiFe] hydrogenase maturation proteins HypC, HypD, and HypE catalyze the insertion and cyanation of the iron center of [NiFe] hydrogenases by an unknown mechanism. We have determined the crystal structures of HypC, HypD, and HypE from Thermococcus kodakaraensis KOD1 at 1.8 A, 2.07 A, and 1.55 A resolution, respectively. The structure of HypD reveals its probable iron binding and active sites for cyanation. An extended conformation of each conserved motif of HypC and HypE allows the essential cysteine residues of both proteins to interact with the active site of HypD. Furthermore, the C-terminal tail of HypE is shown to exist in an ATP-dependent dynamic equilibrium between outward and inward conformations. Unexpectedly, the [4Fe-4S] cluster environment of HypD is quite similar to that of ferredoxin:thioredoxin reductase (FTR), indicating the existence of a redox cascade similar to the FTR system. These results suggest a cyanation reaction mechanism via unique thiol redox signaling in the HypCDE complex.
About this Structure
2Z1C is a Single protein structure of sequence from Thermococcus kodakarensis. Full crystallographic information is available from OCA.
Reference
Crystal structures of [NiFe] hydrogenase maturation proteins HypC, HypD, and HypE: insights into cyanation reaction by thiol redox signaling., Watanabe S, Matsumi R, Arai T, Atomi H, Imanaka T, Miki K, Mol Cell. 2007 Jul 6;27(1):29-40. PMID:17612488 Page seeded by OCA on Sun May 4 19:49:18 2008
