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1ccr

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[[Image:1ccr.gif|left|200px]]
 
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{{Structure
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==STRUCTURE OF RICE FERRICYTOCHROME C AT 2.0 ANGSTROMS RESOLUTION==
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|PDB= 1ccr |SIZE=350|CAPTION= <scene name='initialview01'>1ccr</scene>, resolution 1.5&Aring;
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<StructureSection load='1ccr' size='340' side='right'caption='[[1ccr]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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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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<table><tr><td colspan='2'>[[1ccr]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CCR FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ccr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ccr OCA], [https://pdbe.org/1ccr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ccr RCSB], [https://www.ebi.ac.uk/pdbsum/1ccr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ccr ProSAT]</span></td></tr>
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</table>
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'''STRUCTURE OF RICE FERRICYTOCHROME C AT 2.0 ANGSTROMS RESOLUTION'''
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== Function ==
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[https://www.uniprot.org/uniprot/CYC_ORYSJ CYC_ORYSJ] Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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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.
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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cc/1ccr_consurf.spt"</scriptWhenChecked>
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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].
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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==Reference==
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</jmolCheckbox>
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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]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ccr ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Oryza sativa]]
[[Category: Oryza sativa]]
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[[Category: Single protein]]
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[[Category: Aihara S]]
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[[Category: Aihara, S.]]
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[[Category: Hata Y]]
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[[Category: Hata, Y.]]
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[[Category: Kakudo M]]
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[[Category: Kakudo, M.]]
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[[Category: Morita Y]]
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[[Category: Morita, Y.]]
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[[Category: Ochi H]]
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[[Category: Ochi, H.]]
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[[Category: Sakurai T]]
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[[Category: Sakurai, T.]]
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[[Category: Tanaka N]]
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[[Category: Tanaka, N.]]
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[[Category: ACE]]
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[[Category: HEM]]
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[[Category: TML]]
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[[Category: electron transport(cytochrome)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:22:46 2008''
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Current revision

STRUCTURE OF RICE FERRICYTOCHROME C AT 2.0 ANGSTROMS RESOLUTION

PDB ID 1ccr

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