3VYS
Crystal structure of the HypC-HypD-HypE complex (form I)
Summary for 3VYS
| Entry DOI | 10.2210/pdb3vys/pdb |
| Related | 2Z1C 2Z1D 2Z1E 3VYR 3VYT 3VYU |
| Descriptor | Hydrogenase expression/formation protein HypC, Hydrogenase expression/formation protein HypD, Hydrogenase expression/formation protein HypE, ... (6 entities in total) |
| Functional Keywords | [nife] hydrogenase maturation, metal binding protein-transferase complex, metal binding protein/transferase |
| Biological source | Thermococcus kodakarensis More |
| Total number of polymer chains | 3 |
| Total formula weight | 86438.15 |
| Authors | Watanabe, S.,Miki, K. (deposition date: 2012-10-02, release date: 2012-11-28, Last modification date: 2024-11-13) |
| Primary citation | Watanabe, S.,Matsumi, R.,Atomi, H.,Imanaka, T.,Miki, K. Crystal structures of the HypCD complex and the HypCDE ternary complex: transient intermediate complexes during [NiFe] hydrogenase maturation Structure, 20:2124-2137, 2012 Cited by PubMed Abstract: [NiFe] hydrogenase maturation represents one of the most dynamic and sophisticated processes in metallocenter assembly. The Fe(CN)(2)CO moiety of [NiFe] hydrogenases is assembled via unknown transient interactions among specific maturation proteins HypC (metallochaperone), HypD (redox protein), and HypE (cyanide synthesis/donor). Here, we report the structures of the HypC-HypD and HypC-HypD-HypE complexes, providing a view of the transient interactions that take place during the maturation process. HypC binds to the conserved region of HypD through extensive hydrophobic interactions. The ternary complex formation between HypE and the HypCD complex involves both HypC and HypD, rendering the HypE conformation favorable for cyanide transfer. In the complex, the conserved cysteines of HypC and HypD form an Fe binding site. The conserved C-terminal cysteine of HypE can access the thiol redox cascade of HypD. These results provide structural insights into the Fe atom cyanation in the HypCDE complex. PubMed: 23123111DOI: 10.1016/j.str.2012.09.018 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.35 Å) |
Structure validation
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