Download MendeleyThe crystal structure of wild-type human brain neuroglobin reveals flexibility of the disulfide bond that regulates oxygen affinity.
Guimaraes, B.G., Hamdane, D., Lechauve, C., Marden, M.C., Golinelli-Pimpaneau, B.(2014) Acta Crystallogr D Biol Crystallogr 70: 1005-1014
- PubMed: 24699645
- DOI: https://doi.org/10.1107/S1399004714000078
- Primary Citation of Related Structures:
4MPM - 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?? 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.
Organizational Affiliation:
Synchrotron SOLEIL, L'Orme des Merisiers, Saint-Aubin, 91190 Gif-sur-Yvette, France.
