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 murin...

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Autores principales:	Nathalie Colloc’h, Sophie Sacquin-Mora, Giovanna Avella, Anne-Claire Dhaussy, Thierry Prangé, Beatrice Vallone, Eric Girard
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/f4b2a5527a4d4c15a8d907c3cada4716
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spelling	oai:doaj.org-article:f4b2a5527a4d4c15a8d907c3cada47162021-12-02T12:32:28ZDeterminants of neuroglobin plasticity highlighted by joint coarse-grained simulations and high pressure crystallography10.1038/s41598-017-02097-12045-2322https://doaj.org/article/f4b2a5527a4d4c15a8d907c3cada47162017-05-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-02097-1https://doaj.org/toc/2045-2322Abstract 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.Nathalie Colloc’hSophie Sacquin-MoraGiovanna AvellaAnne-Claire DhaussyThierry PrangéBeatrice ValloneEric GirardNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-10 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Nathalie Colloc’h Sophie Sacquin-Mora Giovanna Avella Anne-Claire Dhaussy Thierry Prangé Beatrice Vallone Eric Girard Determinants of neuroglobin plasticity highlighted by joint coarse-grained simulations and high pressure crystallography
description	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.
format	article
author	Nathalie Colloc’h Sophie Sacquin-Mora Giovanna Avella Anne-Claire Dhaussy Thierry Prangé Beatrice Vallone Eric Girard
author_facet	Nathalie Colloc’h Sophie Sacquin-Mora Giovanna Avella Anne-Claire Dhaussy Thierry Prangé Beatrice Vallone Eric Girard
author_sort	Nathalie Colloc’h
title	Determinants of neuroglobin plasticity highlighted by joint coarse-grained simulations and high pressure crystallography
title_short	Determinants of neuroglobin plasticity highlighted by joint coarse-grained simulations and high pressure crystallography
title_full	Determinants of neuroglobin plasticity highlighted by joint coarse-grained simulations and high pressure crystallography
title_fullStr	Determinants of neuroglobin plasticity highlighted by joint coarse-grained simulations and high pressure crystallography
title_full_unstemmed	Determinants of neuroglobin plasticity highlighted by joint coarse-grained simulations and high pressure crystallography
title_sort	determinants of neuroglobin plasticity highlighted by joint coarse-grained simulations and high pressure crystallography
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/f4b2a5527a4d4c15a8d907c3cada4716
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Determinants of neuroglobin plasticity highlighted by joint coarse-grained simulations and high pressure crystallography

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