2Z1D
Crystal structure of [NiFe] hydrogenase maturation protein, HypD from Thermococcus kodakaraensis
Summary for 2Z1D
| Entry DOI | 10.2210/pdb2z1d/pdb |
| Related | 2Z1C 2Z1E 2Z1F |
| Descriptor | Hydrogenase expression/formation protein hypD, IRON/SULFUR CLUSTER (3 entities in total) |
| Functional Keywords | [nife] hydrogenase maturation, [4fe-4s] cluster, thiol redox, metal binding protein |
| Biological source | Thermococcus kodakarensis |
| Total number of polymer chains | 2 |
| Total formula weight | 84618.65 |
| Authors | Watanabe, S.,Matsumi, R.,Arai, T.,Atomi, H.,Imanaka, T.,Miki, K. (deposition date: 2007-05-08, release date: 2007-07-17, Last modification date: 2024-10-09) |
| Primary citation | Watanabe, S.,Matsumi, R.,Arai, T.,Atomi, H.,Imanaka, T.,Miki, K. Crystal Structures of [NiFe] Hydrogenase Maturation Proteins HypC, HypD, and HypE: Insights into Cyanation Reaction by Thiol Redox Signaling Mol.Cell, 27:29-40, 2007 Cited by PubMed Abstract: [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. PubMed: 17612488DOI: 10.1016/j.molcel.2007.05.039 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.07 Å) |
Structure validation
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