Mapping Hydrophobic Tunnels and Cavities in Neuroglobin with Noble Gas under Pressure.

ABSTRACT: Internal cavities are crucial for conformational flexibility of proteins and can be mapped through noble gas diffusion and docking. Here we investigate the hydrophobic cavities and tunnel network in neuroglobin (Ngb), a hexacoordinated heme protein likely to be involved in neuroprotection, using crystallography under noble gas pressure, mostly at room temperature. In murine Ngb, a large internal cavity is involved in the heme sliding mechanism to achieve binding of gaseous ligands through coordination to the heme iron. In this study, we report that noble gases are hosted by two major sites within the internal cavity. We propose that these cavities could store oxygen and allow its relay in the heme proximity, which could correspond to NO location in the nitrite-reductase function of Ngb. Th

SUBMITTER: Colloc'h N 

PROVIDER: S-EPMC5700381 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature