1giw
From Proteopedia
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|PDB= 1giw |SIZE=350|CAPTION= <scene name='initialview01'>1giw</scene> | |PDB= 1giw |SIZE=350|CAPTION= <scene name='initialview01'>1giw</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=HEC:HEME C'>HEC</scene> | + | |LIGAND= <scene name='pdbligand=HEC:HEME+C'>HEC</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |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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[[Category: Spyroulias, G A.]] | [[Category: Spyroulias, G A.]] | ||
[[Category: Turano, P.]] | [[Category: Turano, P.]] | ||
| - | [[Category: HEC]] | ||
[[Category: cytochrome c]] | [[Category: cytochrome c]] | ||
[[Category: electron transport]] | [[Category: electron transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:44:59 2008'' |
Revision as of 17:45, 30 March 2008
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| Ligands: | |||||||
| Related: | 2GIW
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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