title: Molecular dynamics study of the metallochaperone Hah1 in its apo and Cu(I)-loaded states: role of the conserved residue M10.
abstract: Molecular dynamics simulations were performed on both apo and copper forms of the human copper chaperone, Hah1. Wild-type Hah1 and a methionine (M10) to serine mutant were investigated. We have evidenced the central role of residue M10 in stabilizing the hydrophobic core of Hah1 as well as the internal structure of the metal-binding site. When copper(I) is bound, the mobility of Hah1 is reduced whereas mutation of M10 implies a drastic increase of the mobility of apoHah1, stressing the importance of this highly conserved hydrophobic residue for copper sequestration by the apoprotein.
authors.affiliation: Laboratoire de Biophysique Moléculaire et Cellulaire, Département de Réponse et Dynamique Cellulaires, Commissariat à l'Energie Atomique, Grenoble, France.
authors.forename: David
authors.initials: D
authors.lastname: Poger
authors.forename: Jean-François
authors.initials: JF
authors.lastname: Fuchs
authors.forename: Hristo
authors.initials: H
authors.lastname: Nedev
authors.forename: Michel
authors.initials: M
authors.lastname: Ferrand
authors.forename: Serge
authors.initials: S
authors.lastname: Crouzy
mesh_terms: D001665:Binding Sites; D027682:Cation Transport Proteins / Q000737:chemistry* / Q000378:metabolism; D000079922:Copper Transport Proteins; D056511:Metallochaperones; D008670:Metals / Q000378:metabolism; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry* / Q000378:metabolism; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation
chemical_list: C474500:ATOX1 protein, human; D027682:Cation Transport Proteins; D000079922:Copper Transport Proteins; D056511:Metallochaperones; D008670:Metals; D018832:Molecular Chaperones