1dfs
From Proteopedia
(New page: 200px<br /><applet load="1dfs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dfs" /> '''SOLUTION STRUCTURE OF THE ALPHA-DOMAIN OF MO...) |
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| - | [[Image:1dfs.jpg|left|200px]]<br /><applet load="1dfs" size=" | + | [[Image:1dfs.jpg|left|200px]]<br /><applet load="1dfs" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1dfs" /> | caption="1dfs" /> | ||
'''SOLUTION STRUCTURE OF THE ALPHA-DOMAIN OF MOUSE METALLOTHIONEIN-1'''<br /> | '''SOLUTION STRUCTURE OF THE ALPHA-DOMAIN OF MOUSE METALLOTHIONEIN-1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Sequential 1H-NMR assignments of mouse [Cd7]-metallothionein-1 (MT1) have | + | Sequential 1H-NMR assignments of mouse [Cd7]-metallothionein-1 (MT1) have been carried out by standard homonuclear NMR methods and the use of an accordion-heteronuclear multiple quantum correlation (HMQC) experiment for establishing the metal, 113Cd2+, to cysteine connectivities. The three-dimensional structure was then calculated using the distance constraints from two-dimensional nuclear Overhauser effect (NOE) spectroscopy spectra and the Cys-Cd connectivities as input for a distance geometry-dynamical simulated annealing protocol in X-PLOR 3.851. Similar to the mammalian MT2 isoforms, the homologous primary structure of MT1 suggested two separate domains, each containing one metal cluster. Because there were no interdomain constraints, the structure calculation for the N-terminal beta- and the C-terminal alpha-domain were carried out separately. The structures are based on 409 NMR constraints, consisting of 381 NOEs and 28 cysteine-metal connectivities. The only elements of regular secondary structure found were two short stretches of 3(10) helices along with some half-turns in the alpha-domain. Structural comparison with rat liver MT2 showed high similarity, with the beta-domain structure in mouse MT1 showing evidence of increased flexibility compared to the same domain in MT2. The latter was reflected by the presence of fewer interresidue NOEs, no slowly exchanging backbone amide protons, and enhanced cadmium-cadmium exchange rates found in the beta-domain of MT1. |
==About this Structure== | ==About this Structure== | ||
| - | 1DFS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with CD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1DFS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=CD:'>CD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DFS OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Armitage, I | + | [[Category: Armitage, I M.]] |
| - | [[Category: Otvos, J | + | [[Category: Otvos, J D.]] |
[[Category: Oz, G.]] | [[Category: Oz, G.]] | ||
[[Category: Zangger, K.]] | [[Category: Zangger, K.]] | ||
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[[Category: half turn]] | [[Category: half turn]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:16:15 2008'' |
Revision as of 10:16, 21 February 2008
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SOLUTION STRUCTURE OF THE ALPHA-DOMAIN OF MOUSE METALLOTHIONEIN-1
Overview
Sequential 1H-NMR assignments of mouse [Cd7]-metallothionein-1 (MT1) have been carried out by standard homonuclear NMR methods and the use of an accordion-heteronuclear multiple quantum correlation (HMQC) experiment for establishing the metal, 113Cd2+, to cysteine connectivities. The three-dimensional structure was then calculated using the distance constraints from two-dimensional nuclear Overhauser effect (NOE) spectroscopy spectra and the Cys-Cd connectivities as input for a distance geometry-dynamical simulated annealing protocol in X-PLOR 3.851. Similar to the mammalian MT2 isoforms, the homologous primary structure of MT1 suggested two separate domains, each containing one metal cluster. Because there were no interdomain constraints, the structure calculation for the N-terminal beta- and the C-terminal alpha-domain were carried out separately. The structures are based on 409 NMR constraints, consisting of 381 NOEs and 28 cysteine-metal connectivities. The only elements of regular secondary structure found were two short stretches of 3(10) helices along with some half-turns in the alpha-domain. Structural comparison with rat liver MT2 showed high similarity, with the beta-domain structure in mouse MT1 showing evidence of increased flexibility compared to the same domain in MT2. The latter was reflected by the presence of fewer interresidue NOEs, no slowly exchanging backbone amide protons, and enhanced cadmium-cadmium exchange rates found in the beta-domain of MT1.
About this Structure
1DFS is a Single protein structure of sequence from Mus musculus with as ligand. Full crystallographic information is available from OCA.
Reference
Three-dimensional solution structure of mouse [Cd7]-metallothionein-1 by homonuclear and heteronuclear NMR spectroscopy., Zangger K, Oz G, Otvos JD, Armitage IM, Protein Sci. 1999 Dec;8(12):2630-8. PMID:10631978
Page seeded by OCA on Thu Feb 21 12:16:15 2008
Categories: Mus musculus | Single protein | Armitage, I M. | Otvos, J D. | Oz, G. | Zangger, K. | CD | 3-10 helix | Cd-s cluster | Half turn
