4MPM: Wild-type Human Neuroglobin

Citation:
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 A 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.
PDB ID: 4MPMDownload
MMDB ID: 116672
PDB Deposition Date: 2013/9/13
Updated in MMDB: 2014/05
Experimental Method:
x-ray diffraction
Resolution: 1.74  Å
Source Organism:
Similar Structures:
Biological Unit for 4MPM: dimeric; determined by author and by software (PISA)
Molecular Components in 4MPM
Label Count Molecule
Proteins (2 molecules)
2
Neuroglobin(Gene symbol: NGB)
Molecule annotation
Chemicals (2 molecules)
1
2
* Click molecule labels to explore molecular sequence information.

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