2ZVU
Crystal structure of rat heme oxygenase-1 in complex with ferrous verdoheme
Summary for 2ZVU
| Entry DOI | 10.2210/pdb2zvu/pdb |
| Related | 1DVE 1J2C 1TWN |
| Descriptor | Heme oxygenase 1, 5-OXA-PROTOPORPHYRIN IX CONTAINING FE, FORMIC ACID, ... (4 entities in total) |
| Functional Keywords | reaction intermediate bound structure, oxidoreductase, endoplasmic reticulum, heme, iron, metal-binding, microsome, phosphoprotein |
| Biological source | Rattus norvegicus (Rat) |
| Cellular location | Microsome: P06762 |
| Total number of polymer chains | 1 |
| Total formula weight | 31277.99 |
| Authors | Sato, H.,Sugishima, M.,Fukuyama, K.,Noguchi, M. (deposition date: 2008-11-21, release date: 2009-02-03, Last modification date: 2023-11-01) |
| Primary citation | Sato, H.,Sugishima, M.,Sakamoto, H.,Higashimoto, Y.,Shimokawa, C.,Fukuyama, K.,Palmer, G.,Noguchi, M. Crystal structure of rat haem oxygenase-1 in complex with ferrous verdohaem: presence of a hydrogen-bond network on the distal side Biochem.J., 419:339-345, 2009 Cited by PubMed Abstract: HO (haem oxygenase) catalyses the degradation of haem to biliverdin, CO and ferrous iron via three successive oxygenation reactions, i.e. haem to alpha-hydroxyhaem, alpha-hydroxyhaem to alpha-verdohaem and alpha-verdohaem to ferric biliverdin-iron chelate. In the present study, we determined the crystal structure of ferrous alpha-verdohaem-rat HO-1 complex at 2.2 A (1 A=0.1 nm) resolution. The overall structure of the verdohaem complex was similar to that of the haem complex. Water or OH- was co-ordinated to the verdohaem iron as a distal ligand. A hydrogen-bond network consisting of water molecules and several amino acid residues was observed at the distal side of verdohaem. Such a hydrogen-bond network was conserved in the structures of rat HO-1 complexes with haem and with the ferric biliverdin-iron chelate. This hydrogen-bond network may act as a proton donor to form an activated oxygen intermediate, probably a ferric hydroperoxide species, in the degradation of alpha-verdohaem to ferric biliverdin-iron chelate similar to that seen in the first oxygenation step. PubMed: 19154182DOI: 10.1042/BJ20082279 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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