Influence of NH-Sgamma bonding interactions on the structure and dynamics of metallothioneins.
Mammalian metallothioneins ([Formula: see text]) show a clustered arrangement of the metal ions and a nonregular protein structure. The solution structures of Cd(3)-thiolate cluster containing beta-domain of mouse beta-MT-1 and rat beta-MT-2 show high structural similarities, but widely differing structure dynamics. Molecular dynamics simulations revealed a substantially increased number of NH-Sgamma hydrogen bonds in beta-MT-2, features likely responsible for the increased stability of the Cd(3)-thiolate cluster and the enfolding protein domain. Alterations in the NH-Sgamma hydrogen-bonding network may provide a rationale for the differences in dynamic properties encountered in the beta-domains of MT-1, -2, and -3 isoforms, believed to be essential for their different biological function.
Romero-Isart
Núria
N
Department of Biochemistry, University of Zürich, Winterthurerstrasse 190, CH-8057, Zürich, Switzerland.
Oliva
Baldo
B
Vasák
Milan
M
D000595:Amino Acid Sequence; D000818:Animals; D016000:Cluster Analysis; D006860:Hydrogen Bonding; D008668:Metallothionein / Q000737:chemistry*; D008670:Metals / Q000737:chemistry; D051379:Mice; D008969:Molecular Sequence Data; D009942:Organometallic Compounds / Q000737:chemistry; D010455:Peptides / Q000737:chemistry; D017433:Protein Structure, Secondary; D051381:Rats; D016415:Sequence Alignment; D013997:Time Factors
D008670:Metals; D009942:Organometallic Compounds; D010455:Peptides; D008668:Metallothionein