Molecular dynamics simulation of the neuroglobin crystal: comparison with the simulation in solution.

ABSTRACT: Neuroglobin (Ngb) is a monomeric protein that, despite the small sequence similarity with other globins, displays the typical globin fold. In the absence of exogenous ligands, the ferric and the ferrous forms of Ngb are both hexacoordinated to the distal and proximal histidines. In the ferrous form, oxygen, nitric oxide or carbon monoxide can displace the distal histidine, yielding a reversible adduct. Crystallographic data show that the binding of an exogenous ligand is associated to structural changes involving heme sliding and a topological reorganization of the internal cavities. Molecular dynamics (MD) simulations in solution show that the heme oscillates between two positions, much as the ones observed in the crystal structure, although the occupancy is different. The simulations als

SUBMITTER: Anselmi M 

PROVIDER: S-EPMC2567928 | biostudies-literature | 2008 Nov

REPOSITORIES: biostudies-literature