1giw: Difference between revisions

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[[Image:1giw.jpg|left|200px]]
[[Image:1giw.jpg|left|200px]]


{{Structure
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{{STRUCTURE_1giw| PDB=1giw  | SCENE= }}  
|RELATEDENTRY=[[2giw|2GIW]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1giw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1giw OCA], [http://www.ebi.ac.uk/pdbsum/1giw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1giw RCSB]</span>
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'''SOLUTION STRUCTURE OF REDUCED HORSE HEART CYTOCHROME C, NMR, MINIMIZED AVERAGE STRUCTURE'''
'''SOLUTION STRUCTURE OF REDUCED HORSE HEART CYTOCHROME C, NMR, MINIMIZED AVERAGE STRUCTURE'''
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[[Category: Spyroulias, G A.]]
[[Category: Spyroulias, G A.]]
[[Category: Turano, P.]]
[[Category: Turano, P.]]
[[Category: cytochrome c]]
[[Category: Cytochrome c]]
[[Category: electron transport]]
[[Category: Electron transport]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 17:37:49 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:44:59 2008''

Revision as of 17:37, 2 May 2008

File:1giw.jpg

Template:STRUCTURE 1giw

SOLUTION STRUCTURE OF REDUCED HORSE HEART CYTOCHROME C, NMR, MINIMIZED AVERAGE STRUCTURE


OverviewOverview

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 StructureAbout this Structure

1GIW is a Single protein structure of sequence from Equus caballus. Full crystallographic information is available from OCA.

ReferenceReference

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 Page seeded by OCA on Fri May 2 17:37:49 2008

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