3D solution structure of copper and silver‐substituted yeast metallothioneins

FEBS Letters

Armitage, Ian M.²  Narula, Surinder S.²  Peterson, Cynthia W.¹ 

[1] Physics Department, Univ. of Connecticut, Storrs, CT 06269-3046, USA;Department of Pharmacology, Yale University School of Medicine, 333 Cedar Street, P.O. Box 208066, New Haven, CT 06520-8066, USA

关键词: Yeast metallothionein;    Protein structure;    Nuclear magnetic resonance;    AgMT;    silver(I)-substituted yeast metallothionein;    AgT48;    silver(I)-substituted yeast mutant metallothionein;    COSY;    homonuclear two-dimensional correlation spectroscopy;    CuMT;    copper(I) yeast metallothionein;    EXAFS;    extended X-ray absorption fine structure;    HMQC;    heteronuclear multiple-quantum coherence spectroscopy;    MT;    metallothionein;    NMR;    nuclear magnetic resonance;    NOE;    nuclear Overhauser effect;    rmsd;    root mean square deviation;   

DOI  :  10.1016/0014-5793(95)01492-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

3D solution structural calculations for yeast silver(I)-substituted metallothionein (MT) and native copper(I) MT were completed using experimentally determined NOE and dihedral angle constraints, in conjunction with experimentally derived metal-to-Cys connectivities for AgMT which were assumed identical for CuMT. For the first 40 residues in both structures, the polypeptide backbone wraps around the metal cluster in two large parallel loops separated by a deep cleft containing the metal cluster. Minor differences between the two structures include differences in hydrogen bonds and the orientation of the N-terminus with the overall protein volume conserved to within 6.5%.

【 授权许可】

Unknown