1giw
From Proteopedia
(New page: 200px<br /><applet load="1giw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1giw" /> '''SOLUTION STRUCTURE OF REDUCED HORSE HEART CY...) |
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| - | [[Image:1giw.jpg|left|200px]]<br /><applet load="1giw" size=" | + | [[Image:1giw.jpg|left|200px]]<br /><applet load="1giw" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1giw" /> | caption="1giw" /> | ||
'''SOLUTION STRUCTURE OF REDUCED HORSE HEART CYTOCHROME C, NMR, MINIMIZED AVERAGE STRUCTURE'''<br /> | '''SOLUTION STRUCTURE OF REDUCED HORSE HEART CYTOCHROME C, NMR, MINIMIZED AVERAGE STRUCTURE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | In the frame of a broad study on the structural differences between the | + | In the frame of a broad study on the structural differences between the two redox forms of cytochromes to be related to the electron transfer process, the NMR solution structure of horse heart cytochrome c in the reduced form has been determined. The structural data obtained in the present work are compared to those already available in the literature on the same protein and the presence of conformational differences is discussed in the light of the experimental method employed for the structure determination. Redox-state dependent changes are analyzed and in particular they are related to the role of propionate-7 of the heme. Also some hydrogen bonds are changed upon reduction of the heme iron. A substantial similarity is observed for the backbone fold, independently of the oxidation state. At variance, some meaningful differences are observed in the orientation of a few side chains. These changes are related to those found in the case of the highly homologous cytochrome c from Saccharomyces cerevisiae. The exchangeability of the NH protons has been investigated and found to be smaller than in the case of the oxidized protein. We think that this is a characteristic of reduced cytochromes and that mobility is a medium for molecular recognition in vivo. |
==About this Structure== | ==About this Structure== | ||
| - | 1GIW 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:// | + | 1GIW 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=1GIW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Banci, L.]] | [[Category: Banci, L.]] | ||
[[Category: Bertini, I.]] | [[Category: Bertini, I.]] | ||
| - | [[Category: Huber, J | + | [[Category: Huber, J G.]] |
| - | [[Category: Spyroulias, G | + | [[Category: Spyroulias, G A.]] |
[[Category: Turano, P.]] | [[Category: Turano, P.]] | ||
[[Category: HEC]] | [[Category: HEC]] | ||
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[[Category: electron transport]] | [[Category: electron transport]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:50:34 2008'' |
Revision as of 10:50, 21 February 2008
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SOLUTION STRUCTURE OF REDUCED HORSE HEART CYTOCHROME C, NMR, MINIMIZED AVERAGE STRUCTURE
Overview
In the frame of a broad study on the structural differences between the two redox forms of cytochromes to be related to the electron transfer process, the NMR solution structure of horse heart cytochrome c in the reduced form has been determined. The structural data obtained in the present work are compared to those already available in the literature on the same protein and the presence of conformational differences is discussed in the light of the experimental method employed for the structure determination. Redox-state dependent changes are analyzed and in particular they are related to the role of propionate-7 of the heme. Also some hydrogen bonds are changed upon reduction of the heme iron. A substantial similarity is observed for the backbone fold, independently of the oxidation state. At variance, some meaningful differences are observed in the orientation of a few side chains. These changes are related to those found in the case of the highly homologous cytochrome c from Saccharomyces cerevisiae. The exchangeability of the NH protons has been investigated and found to be smaller than in the case of the oxidized protein. We think that this is a characteristic of reduced cytochromes and that mobility is a medium for molecular recognition in vivo.
About this Structure
1GIW is a Single protein structure of sequence from Equus caballus with as ligand. Full crystallographic information is available from OCA.
Reference
Solution structure of reduced horse heart cytochrome c., Banci L, Bertini I, Huber JG, Spyroulias GA, Turano P, J Biol Inorg Chem. 1999 Feb;4(1):21-31. PMID:10499099
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