Molecular dynamics study of the metallochaperone Hah1 in its apo and Cu(I)-loaded states: Role of the conserved residue M10
- 12 September 2005
- journal article
- Published by Wiley in FEBS Letters
- Vol. 579 (24) , 5287-5292
- https://doi.org/10.1016/j.febslet.2005.08.052
Abstract
International audienceMolecular 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 apoproteinKeywords
This publication has 19 references indexed in Scilit:
- Solution Structure of the Apo and Copper(I)-Loaded Human Metallochaperone HAH1Biochemistry, 2004
- X-ray Absorption Spectroscopy of the Copper Chaperone HAH1 Reveals a Linear Two-coordinate Cu(I) Center Capable of Adduct Formation with Exogenous Thiols and PhosphinesJournal of Biological Chemistry, 2003
- Selectivity in heavy metal‐ binding to peptides and proteinsBiopolymers, 2002
- Metallochaperones and Metal-Transporting ATPases: A Comparative Analysis of Sequences and StructuresGenome Research, 2002
- Copper Trafficking: the Solution Structure of Bacillus subtilis CopZBiochemistry, 2001
- Solution Structure of the Cu(I) and Apo Forms of the Yeast Metallochaperone, Atx1,Biochemistry, 2001
- Structure and chemistry of the copper chaperone proteinsPublished by Elsevier ,2000
- Metal Binding Specificity in Carbonic Anhydrase Is Influenced by Conserved Hydrophobic Core ResiduesBiochemistry, 1999
- Identification and Functional Expression of HAH1, a Novel Human Gene Involved in Copper HomeostasisJournal of Biological Chemistry, 1997
- Where metal ions bind in proteins.Proceedings of the National Academy of Sciences, 1990