FEBS Letters · 2005 · 24 citations · 18 references
Life SciencesBiochemistryMolecular BiologyMolecular BiophysicsProtein BiochemistryStructural BiologyChaperone-assisted FoldingEnzyme StabilityMetal StabilityMetal-ligand BondingMolecular ChaperonesProtein DynamicsCopper Chaperone ProteinsCopper ChaperonesCopper ProteinsCopper-binding SitesHydrophobic Core FormationMetal ChaperonesMetal-binding PropertiesMetal-binding Proteins
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.
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Where metal ions bind in proteins.
M M Yamashita, Laura Wesson, George Eisenman et al. · Proceedings of the National Academy of Sciences · 1990 · 330 citations