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1cgo

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[[Image:1cgo.jpg|left|200px]]<br /><applet load="1cgo" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1cgo, resolution 1.8&Aring;" />
 
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'''CYTOCHROME C''''<br />
 
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==Overview==
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==CYTOCHROME C'==
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The three-dimensional structures of two cytochromes c' have been determined in order to analyse the common features of proteins of this family and their relationship with other four-helix bundle structures. The structure of cytochrome c' from Alcaligenes sp was determined by molecular replacement supplemented with the iron anomalous scattering and the use of a single isomorphous heavy-atom derivative, and was refined using synchrotron data to 1.8 A resolution. The final model, comprising 956 protein atoms (one monomer) and 89 water molecules, has a final R value of 0.188 for all data in the range 20.0-1.8 A resolution (14 673 reflections). The structure of the cytochrome c' from Alcaligenes denitrificans is isomorphous and essentially identical (r.m.s. deviation for all atoms 0.36 A). Although its amino-acid sequence has not been determined chemically, only four differences from that of Alcaligenes sp cytochrome c' were identified by the X-ray analysis. The final model for Alcaligenes denitrificans cytochrome c', comprising 953 protein atoms and 75 water molecules, gave a final R factor of 0.167 for all data in the range 20.0-2.15 A (8220 reflections). The cytochrome c' monomer forms a classic four-helix bundle, determined by the packing of hydrophobic side chains around the enclosed haem group. There are very few cross-linking hydrogen bonds between the helices, the principal side-chain hydrogen bonding involving one of the haem propionates and a conserved Arg residue. The cytochrome c' dimer is created by a crystallographic twofold axis. Monomer-monomer contacts primarily involve the two A helices, with size complementarity of side chains in a central solvent-excluded portion of the interface and hydrogen bonding at the periphery. Both species have a pyroglutamic acid N-terminal residue. The haem iron is five-coordinate, 0.32 A out of the haem plane towards the fifth ligand, His120. The unusual magnetic properties of the Fe atom may be linked to a conserved basic residue, Arg124, adjacent to His120.
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<StructureSection load='1cgo' size='340' side='right'caption='[[1cgo]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1cgo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Alcaligenes_sp. Alcaligenes sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CGO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CGO FirstGlance]. <br>
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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]] 1.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>
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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=1cgo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cgo OCA], [https://pdbe.org/1cgo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cgo RCSB], [https://www.ebi.ac.uk/pdbsum/1cgo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cgo ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CYCP_ALCXX CYCP_ALCXX] Cytochrome c' is the most widely occurring bacterial c-type cytochrome. Cytochromes c' are high-spin proteins and the heme has no sixth ligand. Their exact function is not known.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cg/1cgo_consurf.spt"</scriptWhenChecked>
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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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</jmolCheckbox>
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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=1cgo ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1CGO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Alcaligenes_sp. Alcaligenes sp.] with <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CGO OCA].
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*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Three-dimensional structure of cytochrome c' from two Alcaligenes species and the implications for four-helix bundle structures., Dobbs AJ, Anderson BF, Faber HR, Baker EN, Acta Crystallogr D Biol Crystallogr. 1996 Mar 1;52(Pt 2):356-68. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299707 15299707]
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[[Category: Alcaligenes sp]]
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[[Category: Alcaligenes sp.]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Anderson BF]]
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[[Category: Anderson, B F.]]
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[[Category: Baker EN]]
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[[Category: Baker, E N.]]
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[[Category: Dobbs AJ]]
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[[Category: Dobbs, A J.]]
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[[Category: Faber HR]]
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[[Category: Faber, H R.]]
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[[Category: HEM]]
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[[Category: electron transport (cytochrome)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:05:55 2008''
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Current revision

CYTOCHROME C'

PDB ID 1cgo

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