1lc2
From Proteopedia
(New page: 200px<br /><applet load="1lc2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lc2" /> '''Solution Structure Of Reduced Horse Heart Cy...) |
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'''Solution Structure Of Reduced Horse Heart Cytochrome c in 30% Acetonitrile Solution, NMR 30 Structures'''<br /> | '''Solution Structure Of Reduced Horse Heart Cytochrome c in 30% Acetonitrile Solution, NMR 30 Structures'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The complete solution structure of ferrocytochrome c in 30% | + | The complete solution structure of ferrocytochrome c in 30% acetonitrile/70% water has been determined using high-field 1D and 2D (1)H NMR methods and deposited in the Protein Data Bank with codes 1LC1 and 1LC2. This is the first time a complete solution protein structure has been determined for a protein in nonaqueous media. Ferrocyt c retains a native protein secondary structure (five alpha-helices and two omega loops) in 30% acetonitrile. H18 and M80 residues are the axial heme ligands, as in aqueous solution. Residues believed to be axial heme ligands in the alkaline-like conformers of ferricyt c, specifically H33 and K72, are positioned close to the heme iron. The orientations of both heme propionates are markedly different in 30% acetonitrile/70% water. Comparative structural analysis of reduced cyt c in 30% acetonitrile/70% water solution with cyt c in different environments has given new insight into the cyt c folding mechanism, the electron transfer pathway, and cell apoptosis. |
==About this Structure== | ==About this Structure== | ||
| - | 1LC2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with HEC as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1LC2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with <scene name='pdbligand=HEC:'>HEC</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LC2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Equus caballus]] | [[Category: Equus caballus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Mabrouk, P | + | [[Category: Mabrouk, P A.]] |
| - | [[Category: Sivakolundu, S | + | [[Category: Sivakolundu, S G.]] |
[[Category: HEC]] | [[Category: HEC]] | ||
[[Category: cytochrome c]] | [[Category: cytochrome c]] | ||
[[Category: organic solvent]] | [[Category: organic solvent]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:43:38 2008'' |
Revision as of 11:43, 21 February 2008
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Solution Structure Of Reduced Horse Heart Cytochrome c in 30% Acetonitrile Solution, NMR 30 Structures
Overview
The complete solution structure of ferrocytochrome c in 30% acetonitrile/70% water has been determined using high-field 1D and 2D (1)H NMR methods and deposited in the Protein Data Bank with codes 1LC1 and 1LC2. This is the first time a complete solution protein structure has been determined for a protein in nonaqueous media. Ferrocyt c retains a native protein secondary structure (five alpha-helices and two omega loops) in 30% acetonitrile. H18 and M80 residues are the axial heme ligands, as in aqueous solution. Residues believed to be axial heme ligands in the alkaline-like conformers of ferricyt c, specifically H33 and K72, are positioned close to the heme iron. The orientations of both heme propionates are markedly different in 30% acetonitrile/70% water. Comparative structural analysis of reduced cyt c in 30% acetonitrile/70% water solution with cyt c in different environments has given new insight into the cyt c folding mechanism, the electron transfer pathway, and cell apoptosis.
About this Structure
1LC2 is a Single protein structure of sequence from Equus caballus with as ligand. Full crystallographic information is available from OCA.
Reference
Structure-function relationship of reduced cytochrome c probed by complete solution structure determination in 30% acetonitrile/water solution., Sivakolundu SG, Mabrouk PA, J Biol Inorg Chem. 2003 May;8(5):527-39. Epub 2003 Feb 15. PMID:12764601
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