1ccr: Difference between revisions
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[[Image:1ccr.gif|left|200px]] | [[Image:1ccr.gif|left|200px]] | ||
'''STRUCTURE OF RICE FERRICYTOCHROME C AT 2.0 ANGSTROMS RESOLUTION''' | {{Structure | ||
|PDB= 1ccr |SIZE=350|CAPTION= <scene name='initialview01'>1ccr</scene>, resolution 1.5Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=TML:METHYL PART OF N-TRIMETHYLLYSINE'>TML</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''STRUCTURE OF RICE FERRICYTOCHROME C AT 2.0 ANGSTROMS RESOLUTION''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1CCR is a [ | 1CCR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryza_sativa Oryza sativa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CCR OCA]. | ||
==Reference== | ==Reference== | ||
Structure of rice ferricytochrome c at 2.0 A resolution., Ochi H, Hata Y, Tanaka N, Kakudo M, Sakurai T, Aihara S, Morita Y, J Mol Biol. 1983 May 25;166(3):407-18. PMID:[http:// | Structure of rice ferricytochrome c at 2.0 A resolution., Ochi H, Hata Y, Tanaka N, Kakudo M, Sakurai T, Aihara S, Morita Y, J Mol Biol. 1983 May 25;166(3):407-18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/6304326 6304326] | ||
[[Category: Oryza sativa]] | [[Category: Oryza sativa]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: electron transport(cytochrome)]] | [[Category: electron transport(cytochrome)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:22:46 2008'' | ||
Revision as of 11:22, 20 March 2008
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| , resolution 1.5Å | |||||||
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| Ligands: | , and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF RICE FERRICYTOCHROME C AT 2.0 ANGSTROMS RESOLUTION
OverviewOverview
The crystal structure of ferricytochrome c from rice embryos has been solved by X-ray diffraction to a resolution of 2.0 A, applying a single isomorphous replacement method with anomalous scattering effects. The initial molecular model was built on a graphics display system and was refined by the Hendrickson and Konnert method. The R factor was reduced to 0.25. Rice cytochrome c consists of III amino acid residues. In comparison with animal cytochromes c, the peptide chain extends for eight residues at the N-terminal end, which is characteristic for plant cytochromes c. These additional residues display a collagen-like conformation and an irregular reverse turn, and are located around the C-terminal alpha-helix on the surface or the rear side of the molecule. Two hydrogen bonds between the carbonyl oxygen of the N-terminal acetyl group and O eta of Tyr65, and between the peptide carbonyl oxygen of Pro-1 and O epsilon 1 of Gln89, are involved in holding these eight residues on the molecular surface, where Tyr65 and Gln89 are invariant in plant cytochromes c. Except for the extra eight residues, the main-chain conformations of both rice and tuna cytochromes c are essentially identical, though small local conformational differences are found at residues 24, 25, 56 and 57.
About this StructureAbout this Structure
1CCR is a Single protein structure of sequence from Oryza sativa. Full crystallographic information is available from OCA.
ReferenceReference
Structure of rice ferricytochrome c at 2.0 A resolution., Ochi H, Hata Y, Tanaka N, Kakudo M, Sakurai T, Aihara S, Morita Y, J Mol Biol. 1983 May 25;166(3):407-18. PMID:6304326
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