Three-dimensional structure of rabbit liver [Cd7]metallothionein-2a in aqueous solution determined by nuclear magnetic resonance

Alexandre Arseniev, Peter Schultze, Erich Wörgötter, Werner Braun, Gerhard Wagner, Milan Vašák, Jeremias H R Kägi, Kurt Wüthrich

Research output: Contribution to journalArticle

280 Citations (Scopus)

Abstract

In previous work the metal-polypeptide co-ordinative bonds in the major protein species of a reconstituted [113Cd7]metallothionein-2 preparation from rabbit liver in aqueous solution were determined, the secondary polypeptide structure was found to contain several half-turns and 310-helical segments, and a preliminary characterization of the overall polypeptide backbone fold in the β-domain containing the three-metal cluster, and the α-domain containing the four-metal cluster, was obtained. Using a new, more extensive set of nuclear magnetic resonance data these earlier structures were improved by new structure calculations. The new experimental data consist of distance constraints from measurements of nuclear Overhauser effects, and dihedral angle constraints derived from both coupling constants and nuclear Overhauser effects. The structure calculations were performed with the program DISMAN. Since no information on the orientation of the two domains relative to each other could be obtained, the structure calculations were performed separately for the α-domain and the β-domain. The average of the pairwise root-mean-square distances among the 20 structures with the least residual violations of input constraints was 2.9 Å for the β-domain and 1.4 Å for the a-domain (1 Å = 0.1 nm). The overall chirality of the polypeptide fold is right-handed for the β-domain and left-handed for the α-domain. For each of the seven metal ions the local chirality of the co-ordination of the four cysteinyl Sγ atoms is clearly defined. The improved structures of both domains show the previously noted differences relative to the recently published crystal structure of metallothionein-2a from rat liver.

Original languageEnglish (US)
Pages (from-to)637-657
Number of pages21
JournalJournal of Molecular Biology
Volume201
Issue number3
DOIs
StatePublished - Jun 5 1988
Externally publishedYes

Fingerprint

Metallothionein
Magnetic Resonance Spectroscopy
Metals
Rabbits
Peptides
Liver
Ions
Proteins

ASJC Scopus subject areas

  • Virology

Cite this

Three-dimensional structure of rabbit liver [Cd7]metallothionein-2a in aqueous solution determined by nuclear magnetic resonance. / Arseniev, Alexandre; Schultze, Peter; Wörgötter, Erich; Braun, Werner; Wagner, Gerhard; Vašák, Milan; Kägi, Jeremias H R; Wüthrich, Kurt.

In: Journal of Molecular Biology, Vol. 201, No. 3, 05.06.1988, p. 637-657.

Research output: Contribution to journalArticle

Arseniev, Alexandre ; Schultze, Peter ; Wörgötter, Erich ; Braun, Werner ; Wagner, Gerhard ; Vašák, Milan ; Kägi, Jeremias H R ; Wüthrich, Kurt. / Three-dimensional structure of rabbit liver [Cd7]metallothionein-2a in aqueous solution determined by nuclear magnetic resonance. In: Journal of Molecular Biology. 1988 ; Vol. 201, No. 3. pp. 637-657.
@article{973ab6c1ba284ab38e8bec5b9994438b,
title = "Three-dimensional structure of rabbit liver [Cd7]metallothionein-2a in aqueous solution determined by nuclear magnetic resonance",
abstract = "In previous work the metal-polypeptide co-ordinative bonds in the major protein species of a reconstituted [113Cd7]metallothionein-2 preparation from rabbit liver in aqueous solution were determined, the secondary polypeptide structure was found to contain several half-turns and 310-helical segments, and a preliminary characterization of the overall polypeptide backbone fold in the β-domain containing the three-metal cluster, and the α-domain containing the four-metal cluster, was obtained. Using a new, more extensive set of nuclear magnetic resonance data these earlier structures were improved by new structure calculations. The new experimental data consist of distance constraints from measurements of nuclear Overhauser effects, and dihedral angle constraints derived from both coupling constants and nuclear Overhauser effects. The structure calculations were performed with the program DISMAN. Since no information on the orientation of the two domains relative to each other could be obtained, the structure calculations were performed separately for the α-domain and the β-domain. The average of the pairwise root-mean-square distances among the 20 structures with the least residual violations of input constraints was 2.9 {\AA} for the β-domain and 1.4 {\AA} for the a-domain (1 {\AA} = 0.1 nm). The overall chirality of the polypeptide fold is right-handed for the β-domain and left-handed for the α-domain. For each of the seven metal ions the local chirality of the co-ordination of the four cysteinyl Sγ atoms is clearly defined. The improved structures of both domains show the previously noted differences relative to the recently published crystal structure of metallothionein-2a from rat liver.",
author = "Alexandre Arseniev and Peter Schultze and Erich W{\"o}rg{\"o}tter and Werner Braun and Gerhard Wagner and Milan Vaš{\'a}k and K{\"a}gi, {Jeremias H R} and Kurt W{\"u}thrich",
year = "1988",
month = "6",
day = "5",
doi = "10.1016/0022-2836(88)90644-4",
language = "English (US)",
volume = "201",
pages = "637--657",
journal = "Journal of Molecular Biology",
issn = "0022-2836",
publisher = "Academic Press Inc.",
number = "3",

}

TY - JOUR

T1 - Three-dimensional structure of rabbit liver [Cd7]metallothionein-2a in aqueous solution determined by nuclear magnetic resonance

AU - Arseniev, Alexandre

AU - Schultze, Peter

AU - Wörgötter, Erich

AU - Braun, Werner

AU - Wagner, Gerhard

AU - Vašák, Milan

AU - Kägi, Jeremias H R

AU - Wüthrich, Kurt

PY - 1988/6/5

Y1 - 1988/6/5

N2 - In previous work the metal-polypeptide co-ordinative bonds in the major protein species of a reconstituted [113Cd7]metallothionein-2 preparation from rabbit liver in aqueous solution were determined, the secondary polypeptide structure was found to contain several half-turns and 310-helical segments, and a preliminary characterization of the overall polypeptide backbone fold in the β-domain containing the three-metal cluster, and the α-domain containing the four-metal cluster, was obtained. Using a new, more extensive set of nuclear magnetic resonance data these earlier structures were improved by new structure calculations. The new experimental data consist of distance constraints from measurements of nuclear Overhauser effects, and dihedral angle constraints derived from both coupling constants and nuclear Overhauser effects. The structure calculations were performed with the program DISMAN. Since no information on the orientation of the two domains relative to each other could be obtained, the structure calculations were performed separately for the α-domain and the β-domain. The average of the pairwise root-mean-square distances among the 20 structures with the least residual violations of input constraints was 2.9 Å for the β-domain and 1.4 Å for the a-domain (1 Å = 0.1 nm). The overall chirality of the polypeptide fold is right-handed for the β-domain and left-handed for the α-domain. For each of the seven metal ions the local chirality of the co-ordination of the four cysteinyl Sγ atoms is clearly defined. The improved structures of both domains show the previously noted differences relative to the recently published crystal structure of metallothionein-2a from rat liver.

AB - In previous work the metal-polypeptide co-ordinative bonds in the major protein species of a reconstituted [113Cd7]metallothionein-2 preparation from rabbit liver in aqueous solution were determined, the secondary polypeptide structure was found to contain several half-turns and 310-helical segments, and a preliminary characterization of the overall polypeptide backbone fold in the β-domain containing the three-metal cluster, and the α-domain containing the four-metal cluster, was obtained. Using a new, more extensive set of nuclear magnetic resonance data these earlier structures were improved by new structure calculations. The new experimental data consist of distance constraints from measurements of nuclear Overhauser effects, and dihedral angle constraints derived from both coupling constants and nuclear Overhauser effects. The structure calculations were performed with the program DISMAN. Since no information on the orientation of the two domains relative to each other could be obtained, the structure calculations were performed separately for the α-domain and the β-domain. The average of the pairwise root-mean-square distances among the 20 structures with the least residual violations of input constraints was 2.9 Å for the β-domain and 1.4 Å for the a-domain (1 Å = 0.1 nm). The overall chirality of the polypeptide fold is right-handed for the β-domain and left-handed for the α-domain. For each of the seven metal ions the local chirality of the co-ordination of the four cysteinyl Sγ atoms is clearly defined. The improved structures of both domains show the previously noted differences relative to the recently published crystal structure of metallothionein-2a from rat liver.

UR - http://www.scopus.com/inward/record.url?scp=0023937834&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023937834&partnerID=8YFLogxK

U2 - 10.1016/0022-2836(88)90644-4

DO - 10.1016/0022-2836(88)90644-4

M3 - Article

VL - 201

SP - 637

EP - 657

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 3

ER -