1Q1F
Crystal structure of murine neuroglobin
Summary for 1Q1F
| Entry DOI | 10.2210/pdb1q1f/pdb |
| Descriptor | Neuroglobin, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total) |
| Functional Keywords | globin fold, heme protein, neuroglobin, oxygen storage-transport complex, oxygen storage/transport |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 17640.78 |
| Authors | Vallone, B.,Nienhaus, K.,Matthes, K.,Brunori, M.,Nienhaus, G.U. (deposition date: 2003-07-19, release date: 2004-06-08, Last modification date: 2024-02-14) |
| Primary citation | Vallone, B.,Nienhaus, K.,Brunori, M.,Nienhaus, G.U. The structure of murine neuroglobin: Novel pathways for ligand migration and binding. Proteins, 56:85-92, 2004 Cited by PubMed Abstract: Neuroglobin, a recently discovered globin predominantly expressed in neuronal tissue of vertebrates, binds small, gaseous ligands at the sixth coordination position of the heme iron. In the absence of an exogenous ligand, the distal histidine (His64) binds to the heme iron in the ferrous and ferric states. The crystal structure of murine ferric (met) neuroglobin at 1.5 A reveals interesting features relevant to the ligand binding mechanism. Only weak selectivity is observed for the two possible heme orientations, the occupancy ratio being 70:30. Two small internal cavities are present on the heme distal side, which enable the His64(E7) side chain to move out of the way upon exogenous ligand binding. Moreover, a third, huge cavity (volume approximately 290 A3) connecting both sides of the heme, is open towards the exterior and provides a potential passageway for ligands. The CD and EF corners exhibit substantial flexibility, which may assist ligands in entering the protein and accessing the active site. Based on this high-resolution structure, further structure-function studies can be planned to elucidate the role of neuroglobin in physiological responses to hypoxia. PubMed: 15162488DOI: 10.1002/prot.20113 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
Download full validation report
