1fi7
From Proteopedia
(New page: 200px<br /><applet load="1fi7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fi7" /> '''Solution structure of the imidazole complex ...) |
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| - | [[Image:1fi7.gif|left|200px]]<br /><applet load="1fi7" size=" | + | [[Image:1fi7.gif|left|200px]]<br /><applet load="1fi7" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''Solution structure of the imidazole complex of cytochrome C'''<br /> | '''Solution structure of the imidazole complex of cytochrome C'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Although imidazole ligand binding to cytochrome c is not directly related | + | Although imidazole ligand binding to cytochrome c is not directly related to its physiological function, it has the potential to provide valuable information on the molecular and electronic structure of the protein. The solution structure of the imidazole adduct of oxidized horse heart cytochrome c (Im-cyt c) has been determined through 2D NMR spectroscopy. The Im-cyt c, 8 mM in 1.2 M imidazole solution at pH 5.7 and 313 K, provided altogether 2,542 NOEs (1,901 meaningful NOEs) and 194 pseudocontact shifts. The 35 conformers of the family show the RMSD values to the average structure of 0.063+/-0.007 nm for the backbone and 0.107+/-0.007 nm for all heavy atoms, respectively. The characterization of Im-cyt c is discussed in detail both in terms of structure and electronic properties. The replacement of the axial ligand Met80 with the exogenous imidazole ligand induces significant conformation changes in both backbone and side chains of the residues located in the distal axial ligand regions. The imidazole ligand binds essentially parallel to the imidazole of the proximal histidine, the two planes forming an angle of 8+/-7 degrees. The electron delocalization on the heme moiety and the magnetic susceptibility tensor are consistent with these structural features. |
==About this Structure== | ==About this Structure== | ||
| - | 1FI7 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 IMD and HEC as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1FI7 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=IMD:'>IMD</scene> and <scene name='pdbligand=HEC:'>HEC</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FI7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: solution structure]] | [[Category: solution structure]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:38:56 2008'' |
Revision as of 10:38, 21 February 2008
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Solution structure of the imidazole complex of cytochrome C
Overview
Although imidazole ligand binding to cytochrome c is not directly related to its physiological function, it has the potential to provide valuable information on the molecular and electronic structure of the protein. The solution structure of the imidazole adduct of oxidized horse heart cytochrome c (Im-cyt c) has been determined through 2D NMR spectroscopy. The Im-cyt c, 8 mM in 1.2 M imidazole solution at pH 5.7 and 313 K, provided altogether 2,542 NOEs (1,901 meaningful NOEs) and 194 pseudocontact shifts. The 35 conformers of the family show the RMSD values to the average structure of 0.063+/-0.007 nm for the backbone and 0.107+/-0.007 nm for all heavy atoms, respectively. The characterization of Im-cyt c is discussed in detail both in terms of structure and electronic properties. The replacement of the axial ligand Met80 with the exogenous imidazole ligand induces significant conformation changes in both backbone and side chains of the residues located in the distal axial ligand regions. The imidazole ligand binds essentially parallel to the imidazole of the proximal histidine, the two planes forming an angle of 8+/-7 degrees. The electron delocalization on the heme moiety and the magnetic susceptibility tensor are consistent with these structural features.
About this Structure
1FI7 is a Single protein structure of sequence from Equus caballus with and as ligands. Full crystallographic information is available from OCA.
Reference
Effects of extrinsic imidazole ligation on the molecular and electronic structure of cytochrome c., Banci L, Bertini I, Liu G, Lu J, Reddig T, Tang W, Wu Y, Yao Y, Zhu D, J Biol Inorg Chem. 2001 Jun;6(5-6):628-37. PMID:11472026
Page seeded by OCA on Thu Feb 21 12:38:56 2008
Categories: Equus caballus | Single protein | Banci, L. | Bertini, I. | Liu, G. | Lu, J. | Reddig, T. | Tang, W. | Wu, Y. | Zhu, D. | HEC | IMD | Cytochrome c | Nmr | Solution structure
