1ccr: Difference between revisions

Revision as of 13:04, 21 February 2008

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 with , and as ligands. 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

Page seeded by OCA on Thu Feb 21 12:04:45 2008

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OCA

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-[[Image:1ccr.gif|left|200px]]<br /><applet load="1ccr" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1ccr.gif|left|200px]]<br /><applet load="1ccr" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1ccr, resolution 1.5&Aring;" />
 '''STRUCTURE OF RICE FERRICYTOCHROME C AT 2.0 ANGSTROMS RESOLUTION'''<br />
 ==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.
+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==
-CCR 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 ACE, HEM and TML as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CCR OCA].
+CCR 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].
 ==Reference==
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 [[Category: electron transport(cytochrome)]]
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