Determinants of neuroglobin plasticity highlighted by joint coarse-grained simulations and high pressure crystallography. - Université Denis Diderot - Paris VII
Article Dans Une Revue Scientific Reports Année : 2017

Determinants of neuroglobin plasticity highlighted by joint coarse-grained simulations and high pressure crystallography.

Résumé

Investigating the effect of pressure sheds light on the dynamics and plasticity of proteins, intrinsically correlated to functional efficiency. Here we detail the structural response to pressure of neuroglobin (Ngb), a hexacoordinate globin likely to be involved in neuroprotection. In murine Ngb, reversible coordination is achieved by repositioning the heme more deeply into a large internal cavity, the “heme sliding mechanism”. Combining high pressure crystallography and coarse-grain simulations on wild type Ngb as well as two mutants, one (V101F) with unaffected and another (F106W) with decreased affinity for CO, we show that Ngb hinges around a rigid mechanical nucleus of five hydrophobic residues (V68, I72, V109, L113, Y137) during its conformational transition induced by gaseous ligand, that the intrinsic flexibility of the F-G loop appears essential to drive the heme sliding mechanism, and that residue Val 101 may act as a sensor of the interaction disruption between the heme and the distal histidine.
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Dates et versions

hal-01523850 , version 1 (18-12-2024)

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Nathalie Colloc’h, Sophie Sacquin-Mora, Giovanna Avella, Anne-Claire Dhaussy, Thierry Prangé, et al.. Determinants of neuroglobin plasticity highlighted by joint coarse-grained simulations and high pressure crystallography.. Scientific Reports, 2017, 7 (1), pp.1858. ⟨10.1038/s41598-017-02097-1⟩. ⟨hal-01523850⟩
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