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1ccr

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[[Image:1ccr.gif|left|200px]]<br /><applet load="1ccr" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ccr.gif|left|200px]]
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caption="1ccr, resolution 1.5&Aring;" />
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'''STRUCTURE OF RICE FERRICYTOCHROME C AT 2.0 ANGSTROMS RESOLUTION'''<br />
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{{Structure
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|PDB= 1ccr |SIZE=350|CAPTION= <scene name='initialview01'>1ccr</scene>, resolution 1.5&Aring;
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|SITE=
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|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>
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|ACTIVITY=
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|GENE=
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}}
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'''STRUCTURE OF RICE FERRICYTOCHROME C AT 2.0 ANGSTROMS RESOLUTION'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1CCR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryza_sativa Oryza sativa] with <scene name='pdbligand=ACE:'>ACE</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=TML:'>TML</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CCR OCA].
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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==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=6304326 6304326]
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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)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:04:45 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:22:46 2008''

Revision as of 08:22, 20 March 2008


PDB ID 1ccr

Drag the structure with the mouse to rotate
, resolution 1.5Å
Ligands: , and
Coordinates: save as pdb, mmCIF, xml



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

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