1ccr

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[[Image:1ccr.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1ccr", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=TML:METHYL+PART+OF+N-TRIMETHYLLYSINE'>TML</scene>
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{{STRUCTURE_1ccr| PDB=1ccr | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ccr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ccr OCA], [http://www.ebi.ac.uk/pdbsum/1ccr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ccr RCSB]</span>
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'''STRUCTURE OF RICE FERRICYTOCHROME C AT 2.0 ANGSTROMS RESOLUTION'''
'''STRUCTURE OF RICE FERRICYTOCHROME C AT 2.0 ANGSTROMS RESOLUTION'''
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[[Category: Sakurai, T.]]
[[Category: Sakurai, T.]]
[[Category: Tanaka, N.]]
[[Category: Tanaka, N.]]
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[[Category: electron transport(cytochrome)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:35:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:19:09 2008''
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Revision as of 09:35, 2 May 2008

Image:1ccr.gif

Template:STRUCTURE 1ccr

STRUCTURE OF RICE FERRICYTOCHROME C AT 2.0 ANGSTROMS RESOLUTION


Overview

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 Structure

1CCR is a Single protein structure of sequence from Oryza sativa. Full crystallographic information is available from OCA.

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:6304326 Page seeded by OCA on Fri May 2 12:35:22 2008

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