1ig5

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==Overview==
==Overview==
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The three-dimensional structures of the magnesium- and manganese-bound, forms of calbindin D9k were determined to 1.6 A and 1.9 A resolution, respectively, using X-ray crystallography. These two structures are nearly, identical but deviate significantly from both the calcium bound form and, the metal ion-free (apo) form. The largest structural differences are seen, in the C-terminal EF-hand, and involve changes in both metal ion, coordination and helix packing. The N-terminal calcium binding site is not, occupied by any metal ion in the magnesium and manganese structures, and, shows little structural deviation from the apo and calcium bound forms., 1H-NMR and UV spectroscopic studies at physiological ion concentrations, show that the C-terminal site of the protein is significantly populated by, magnesium at resting cell calcium levels, and that there is a negative, allosteric interaction between magnesium and calcium binding. Calcium, binding was found to occur with positive cooperativity at physiological, magnesium concentration.
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The three-dimensional structures of the magnesium- and manganese-bound forms of calbindin D9k were determined to 1.6 A and 1.9 A resolution, respectively, using X-ray crystallography. These two structures are nearly identical but deviate significantly from both the calcium bound form and the metal ion-free (apo) form. The largest structural differences are seen in the C-terminal EF-hand, and involve changes in both metal ion coordination and helix packing. The N-terminal calcium binding site is not occupied by any metal ion in the magnesium and manganese structures, and shows little structural deviation from the apo and calcium bound forms. 1H-NMR and UV spectroscopic studies at physiological ion concentrations show that the C-terminal site of the protein is significantly populated by magnesium at resting cell calcium levels, and that there is a negative allosteric interaction between magnesium and calcium binding. Calcium binding was found to occur with positive cooperativity at physiological magnesium concentration.
==About this Structure==
==About this Structure==
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1IG5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure superseeds the now removed PDB entry 5ICB. Known structural/functional Site: <scene name='pdbsite=MUM:Mg+Binding+Ef-Hand+Loop'>MUM</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IG5 OCA].
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1IG5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 5ICB. Known structural/functional Site: <scene name='pdbsite=MUM:Mg+Binding+Ef-Hand+Loop'>MUM</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IG5 OCA].
==Reference==
==Reference==
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Andersson, E.M.]]
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[[Category: Andersson, E M.]]
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[[Category: Svensson, L.A.]]
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[[Category: Svensson, L A.]]
[[Category: MG]]
[[Category: MG]]
[[Category: calcium-binding protein]]
[[Category: calcium-binding protein]]
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[[Category: magnesium binding]]
[[Category: magnesium binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:50:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:11:33 2008''

Revision as of 11:11, 21 February 2008


1ig5, resolution 1.50Å

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BOVINE CALBINDIN D9K BINDING MG2+

Overview

The three-dimensional structures of the magnesium- and manganese-bound forms of calbindin D9k were determined to 1.6 A and 1.9 A resolution, respectively, using X-ray crystallography. These two structures are nearly identical but deviate significantly from both the calcium bound form and the metal ion-free (apo) form. The largest structural differences are seen in the C-terminal EF-hand, and involve changes in both metal ion coordination and helix packing. The N-terminal calcium binding site is not occupied by any metal ion in the magnesium and manganese structures, and shows little structural deviation from the apo and calcium bound forms. 1H-NMR and UV spectroscopic studies at physiological ion concentrations show that the C-terminal site of the protein is significantly populated by magnesium at resting cell calcium levels, and that there is a negative allosteric interaction between magnesium and calcium binding. Calcium binding was found to occur with positive cooperativity at physiological magnesium concentration.

About this Structure

1IG5 is a Single protein structure of sequence from Bos taurus with as ligand. This structure supersedes the now removed PDB entry 5ICB. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Structural basis for the negative allostery between Ca(2+)- and Mg(2+)-binding in the intracellular Ca(2+)-receptor calbindin D9k., Andersson M, Malmendal A, Linse S, Ivarsson I, Forsen S, Svensson LA, Protein Sci. 1997 Jun;6(6):1139-47. PMID:9194174

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