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

Abstract : 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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Scientific Reports, Nature Publishing Group, 2017, 7 (1), pp.1858. 〈10.1038/s41598-017-02097-1〉
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Soumis le : mercredi 17 mai 2017 - 09:59:50
Dernière modification le : lundi 8 octobre 2018 - 17:44:07

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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, Nature Publishing Group, 2017, 7 (1), pp.1858. 〈10.1038/s41598-017-02097-1〉. 〈hal-01523850〉

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