2mrb: Difference between revisions
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'''THREE-DIMENSIONAL STRUCTURE OF RABBIT LIVER CD-7 METALLOTHIONEIN-2A IN AQUEOUS SOLUTION DETERMINED BY NUCLEAR MAGNETIC RESONANCE''' | '''THREE-DIMENSIONAL STRUCTURE OF RABBIT LIVER CD-7 METALLOTHIONEIN-2A IN AQUEOUS SOLUTION DETERMINED BY NUCLEAR MAGNETIC RESONANCE''' | ||
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[[Category: Woergoetter, E.]] | [[Category: Woergoetter, E.]] | ||
[[Category: Wuthrich, K.]] | [[Category: Wuthrich, K.]] | ||
[[Category: | [[Category: Metallothionein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:34:22 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 09:34, 4 May 2008
THREE-DIMENSIONAL STRUCTURE OF RABBIT LIVER CD-7 METALLOTHIONEIN-2A IN AQUEOUS SOLUTION DETERMINED BY NUCLEAR MAGNETIC RESONANCE
OverviewOverview
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 3(10)-helical segments, and a preliminary characterization of the overall polypeptide backbone fold in the beta-domain containing the three-metal cluster, and the alpha-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 alpha-domain and the beta-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 A for the beta-domain and 1.4 A for the alpha-domain (1 A = 0.1 nm). The overall chirality of the polypeptide fold is right-handed for the beta-domain and left-handed for the alpha-domain. For each of the seven metal ions the local chirality of the co-ordination of the four cysteinyl Sy 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.
About this StructureAbout this Structure
2MRB is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.
ReferenceReference
Three-dimensional structure of rabbit liver [Cd7]metallothionein-2a in aqueous solution determined by nuclear magnetic resonance., Arseniev A, Schultze P, Worgotter E, Braun W, Wagner G, Vasak M, Kagi JH, Wuthrich K, J Mol Biol. 1988 Jun 5;201(3):637-57. PMID:3418714 Page seeded by OCA on Sun May 4 09:34:22 2008