1n9c
From Proteopedia
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|PDB= 1n9c |SIZE=350|CAPTION= <scene name='initialview01'>1n9c</scene> | |PDB= 1n9c |SIZE=350|CAPTION= <scene name='initialview01'>1n9c</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=[[1k3g|1K3G]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n9c OCA], [http://www.ebi.ac.uk/pdbsum/1n9c PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1n9c RCSB]</span> | ||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Bertini, I.]] | [[Category: Bertini, I.]] | ||
[[Category: Rosato, A.]] | [[Category: Rosato, A.]] | ||
| - | [[Category: HEC]] | ||
[[Category: cytochrome c]] | [[Category: cytochrome c]] | ||
[[Category: electron transfer]] | [[Category: electron transfer]] | ||
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[[Category: respiration]] | [[Category: respiration]] | ||
| - | ''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 22:27:10 2008'' |
Revision as of 19:27, 30 March 2008
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| Ligands: | |||||||
| Related: | 1K3G
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure and dynamics of reduced Bacillus pasteurii cytochrome c: oxidation state dependent properties and implications for electron transfer processes
Overview
The solution structure of reduced Bacillus pasteurii cytochrome c, which has only 71 amino acids, has been determined by NMR to an RMSD of 0.46 +/- 0.08 A for all backbone atoms and 0.79 +/- 0.08 A for all heavy atoms and refined through restrained energy minimization. The target function out of 1645 constraints is 0.52 +/- 0.11 A(2), and the penalty function is 66 +/- 12 kJ mol(-)(1). The structure appears very similar to that in the oxidized state, only Trp87 and the propionates showing significant differences. The mobility was investigated through (15)N R(1) and R(2) relaxation rates, (15)N-(1)H NOE, and (1)H/(2)H exchange. It is found that the oxidized form is generally more mobile than the reduced one. By comparing the redox-state dependence of the structural/dynamic properties of Fe-S proteins, cytochrome c, and blue copper proteins, hints are provided for a better comprehension of the electron transfer processes.
About this Structure
1N9C is a Single protein structure of sequence from Sporosarcina pasteurii. Full crystallographic information is available from OCA.
Reference
Structure and dynamics of reduced Bacillus pasteurii cytochrome c: oxidation state dependent properties and implications for electron transfer processes., Bartalesi I, Bertini I, Rosato A, Biochemistry. 2003 Jan 28;42(3):739-45. PMID:12534286
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