1qjl
From Proteopedia
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==Overview== | ==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 . | + | 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 and thus emphasize the special, role of the cysteine residues in defining the structure of, metallothioneins, both on the level of the domain architecture and the, topology of the metal-thiolate clusters. |
==About this Structure== | ==About this Structure== | ||
| - | 1QJL is a | + | 1QJL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Strongylocentrotus_purpuratus Strongylocentrotus purpuratus] with CD as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: CD3. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QJL OCA]. |
==Reference== | ==Reference== | ||
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[[Category: radical scavenger]] | [[Category: radical scavenger]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:03:17 2007'' |
Revision as of 11:57, 5 November 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 and thus emphasize the special, role of the cysteine residues in defining the structure of, metallothioneins, both on the level of the domain architecture and the, topology of the metal-thiolate clusters.
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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