1j5m
From Proteopedia
(New page: 200px<br /><applet load="1j5m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1j5m" /> '''SOLUTION STRUCTURE OF THE SYNTHETIC 113CD_3 ...) |
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caption="1j5m" /> | caption="1j5m" /> | ||
'''SOLUTION STRUCTURE OF THE SYNTHETIC 113CD_3 BETA_N DOMAIN OF LOBSTER METALLOTHIONEIN-1'''<br /> | '''SOLUTION STRUCTURE OF THE SYNTHETIC 113CD_3 BETA_N DOMAIN OF LOBSTER METALLOTHIONEIN-1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structures of the isolated Cd(3)beta domains from | + | The three-dimensional structures of the isolated Cd(3)beta domains from Homarus americanus metallothionein have been determined by NMR methods in order to establish a set of beta-domain structures for comparative analysis. First, it was determined that the Cd-cysteine connectivities forming the Cd(3)S(9) metal center were identical to those observed for the beta(N) domain in the native holoprotein. Time- and temperature-dependence studies of the (113)Cd and (1)H 1D-NMR spectra indicated that the beta(N) domain undergoes slow conformational changes before reaching an equilibrium structure. In addition to structural information provided by the metal-to-cysteine connectivities, Phi, chi(1) and chi(2) angle constraints, three H(N...)S hydrogen bond interactions were also determined from a long-range optimized (1)H(N)-(113)Cd HMQC experiment. A simulated annealing protocol was applied to the distance and angle constraints obtained from the 2D-NMR experiments to calculate the three-dimensional structure of the synthetic Cd(3)beta(N) domain of lobster metallothionein. Structure-reactivity relationships are proposed for the reactions of Cd(3)beta domains with 5,5'-dithiobis(2-nitrobenzoate), based on comparisons of surface exposure of sulfur atoms of the lobster and rabbit Cd(3)beta domain structures. Finally, the surface exposure of the beta domains of lobster is compared with beta domains from mammalian metallothioneins. |
==About this Structure== | ==About this Structure== | ||
| - | 1J5M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with CD as [http://en.wikipedia.org/wiki/ligand ligand]. This structure | + | 1J5M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=CD:'>CD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 1HZR. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J5M OCA]. |
==Reference== | ==Reference== | ||
Structure of the (113)Cd(3)beta domains from Homarus americanus metallothionein-1: hydrogen bonding and solvent accessibility of sulfur atoms., Munoz A, Forsterling FH, Shaw CF 3rd, Petering DH, J Biol Inorg Chem. 2002 Sep;7(7-8):713-24. Epub 2002 Mar 13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12203008 12203008] | Structure of the (113)Cd(3)beta domains from Homarus americanus metallothionein-1: hydrogen bonding and solvent accessibility of sulfur atoms., Munoz A, Forsterling FH, Shaw CF 3rd, Petering DH, J Biol Inorg Chem. 2002 Sep;7(7-8):713-24. Epub 2002 Mar 13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12203008 12203008] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Forsterling, F | + | [[Category: Forsterling, F H.]] |
| - | [[Category: III, C | + | [[Category: III, C F.Shaw.]] |
[[Category: Munoz, A.]] | [[Category: Munoz, A.]] | ||
| - | [[Category: Petering, D | + | [[Category: Petering, D H.]] |
[[Category: CD]] | [[Category: CD]] | ||
[[Category: 113cd-nmr]] | [[Category: 113cd-nmr]] | ||
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[[Category: metallothionein]] | [[Category: metallothionein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:19:08 2008'' |
Revision as of 11:19, 21 February 2008
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SOLUTION STRUCTURE OF THE SYNTHETIC 113CD_3 BETA_N DOMAIN OF LOBSTER METALLOTHIONEIN-1
Overview
The three-dimensional structures of the isolated Cd(3)beta domains from Homarus americanus metallothionein have been determined by NMR methods in order to establish a set of beta-domain structures for comparative analysis. First, it was determined that the Cd-cysteine connectivities forming the Cd(3)S(9) metal center were identical to those observed for the beta(N) domain in the native holoprotein. Time- and temperature-dependence studies of the (113)Cd and (1)H 1D-NMR spectra indicated that the beta(N) domain undergoes slow conformational changes before reaching an equilibrium structure. In addition to structural information provided by the metal-to-cysteine connectivities, Phi, chi(1) and chi(2) angle constraints, three H(N...)S hydrogen bond interactions were also determined from a long-range optimized (1)H(N)-(113)Cd HMQC experiment. A simulated annealing protocol was applied to the distance and angle constraints obtained from the 2D-NMR experiments to calculate the three-dimensional structure of the synthetic Cd(3)beta(N) domain of lobster metallothionein. Structure-reactivity relationships are proposed for the reactions of Cd(3)beta domains with 5,5'-dithiobis(2-nitrobenzoate), based on comparisons of surface exposure of sulfur atoms of the lobster and rabbit Cd(3)beta domain structures. Finally, the surface exposure of the beta domains of lobster is compared with beta domains from mammalian metallothioneins.
About this Structure
1J5M is a Single protein structure of sequence from [1] with as ligand. This structure supersedes the now removed PDB entry 1HZR. Full crystallographic information is available from OCA.
Reference
Structure of the (113)Cd(3)beta domains from Homarus americanus metallothionein-1: hydrogen bonding and solvent accessibility of sulfur atoms., Munoz A, Forsterling FH, Shaw CF 3rd, Petering DH, J Biol Inorg Chem. 2002 Sep;7(7-8):713-24. Epub 2002 Mar 13. PMID:12203008
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