1qjl
From Proteopedia
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Revision as of 13:55, 30 October 2007
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METALLOTHIONEIN MTA FROM SEA URCHIN (BETA DOMAIN)
Overview
The three-dimensional structure of [(113)Cd7]-metallothionein-A (MTA) of, the sea urchin Strongylocentrotus purpuratus was determined by, homonuclear(1)H NMR experiments and heteronuclear [(1)H, (113)Cd]-correlation spectroscopy. MTA is composed of two globular, domains, an N-terminal four-metal domain of the amino acid residues 1 to, 36 and a Cd4Cys11cluster, and a C-terminal three-metal domain including, the amino acid residues 37 to 65 and a Cd3Cys9cluster. The structure, resembles the known mammalian and crustacean metallothioneins, but has a, significantly different connectivity pattern of the Cys-metal, co-ordination bonds and concomitantly contains novel local folds of some, polypeptide backbone segments. These differences can be related to, variations of the Cys sequence positions ... [(full description)]
About this Structure
1QJL is a [Single protein] structure of sequence from [Strongylocentrotus purpuratus] with CD as [ligand]. Structure known Active Site: CD3. Full crystallographic information is available from [OCA].
Reference
NMR structure of the sea urchin (Strongylocentrotus purpuratus) metallothionein MTA., Riek R, Precheur B, Wang Y, Mackay EA, Wider G, Guntert P, Liu A, Kagi JH, Wuthrich K, J Mol Biol. 1999 Aug 13;291(2):417-28. PMID:10438629
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