4MPM
Wild-type human neuroglobin
Summary for 4MPM
| Entry DOI | 10.2210/pdb4mpm/pdb |
| Related | 1OJ6 |
| Descriptor | Neuroglobin, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total) |
| Functional Keywords | globin, oxygen supply, nitrite reductase, proto-porphyrin ix, brain neurons, apoptosis |
| Biological source | Homo sapiens (human) |
| Cellular location | Perikaryon (By similarity): Q9NPG2 |
| Total number of polymer chains | 2 |
| Total formula weight | 35135.72 |
| Authors | Guimaraes, B.G.,Golinelli-Pimpaneau, B. (deposition date: 2013-09-13, release date: 2014-01-15, Last modification date: 2024-11-06) |
| Primary citation | Guimaraes, B.G.,Hamdane, D.,Lechauve, C.,Marden, M.C.,Golinelli-Pimpaneau, B. The crystal structure of wild-type human brain neuroglobin reveals flexibility of the disulfide bond that regulates oxygen affinity. Acta Crystallogr.,Sect.D, 70:1005-1014, 2014 Cited by PubMed Abstract: Neuroglobin plays an important function in the supply of oxygen in nervous tissues. In human neuroglobin, a cysteine at position 46 in the loop connecting the C and D helices of the globin fold is presumed to form an intramolecular disulfide bond with Cys55. Rupture of this disulfide bridge stabilizes bi-histidyl haem hexacoordination, causing an overall decrease in the affinity for oxygen. Here, the first X-ray structure of wild-type human neuroglobin is reported at 1.74 Å resolution. This structure provides a direct observation of two distinct conformations of the CD region containing the intramolecular disulfide link and highlights internal cavities that could be involved in ligand migration and/or are necessary to enable the conformational transition between the low and high oxygen-affinity states following S-S bond formation. PubMed: 24699645DOI: 10.1107/S1399004714000078 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.74 Å) |
Structure validation
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