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1kx2

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[[Image:1kx2.gif|left|200px]]
 
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{{Structure
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==Minimized average structure of a mono-heme ferrocytochrome c from Shewanella putrefaciens==
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|PDB= 1kx2 |SIZE=350|CAPTION= <scene name='initialview01'>1kx2</scene>
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<StructureSection load='1kx2' size='340' side='right'caption='[[1kx2]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=HEC:HEME C'>HEC</scene>
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<table><tr><td colspan='2'>[[1kx2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Shewanella_putrefaciens Shewanella putrefaciens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KX2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KX2 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">Solution NMR</td></tr>
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|GENE= ScyA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=24 Shewanella putrefaciens])
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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></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=1kx2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kx2 OCA], [https://pdbe.org/1kx2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kx2 RCSB], [https://www.ebi.ac.uk/pdbsum/1kx2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kx2 ProSAT]</span></td></tr>
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</table>
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'''Minimized average structure of a mono-heme ferrocytochrome c from Shewanella putrefaciens'''
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== Function ==
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[https://www.uniprot.org/uniprot/O52685_SHEPU O52685_SHEPU]
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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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Within the frame of the characterization of the structure and function of cytochromes c, an 81-amino acid cytochrome c was identified in the genome of Shewanella putrefaciens. Because of the scarce information about bacterial cytochromes of this type and the large variability in sequences and possibly function, we decided to proceed to its structural characterization. This protein was expressed in Escherichia coli and purified. The oxidized species is largely high spin, with a detached methionine, whereas the reduced species has the classical His/Met axial ligation to iron. The NMR solution structure of the reduced form was determined on a (15)N-labeled sample, for which 99% of all non-proline backbone (1)H and (15)N resonances have been assigned. One thousand three hundred two meaningful NOEs, out of 1775 NOEs, together with 66 dihedral angles provide a structure with rmsd values from the mean of 0.50 and 0.96 A for backbone and all heavy atoms, respectively. A search of gene banks allowed us to locate 10 different cytochromes c, the sequences of which are more than 30% identical to that of the S. putrefacienscytochrome. For two of them, the structures are known. The structures of the others have been modeled by using the available templates and internally validated. Structural similarities in terms of surface properties account for their biophysical features and provide hints about the function.
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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/kx/1kx2_consurf.spt"</scriptWhenChecked>
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1KX2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Shewanella_putrefaciens Shewanella putrefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KX2 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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Solution structure of a monoheme ferrocytochrome c from Shewanella putrefaciens and structural analysis of sequence-similar proteins: functional implications., Bartalesi I, Bertini I, Hajieva P, Rosato A, Vasos PR, Biochemistry. 2002 Apr 23;41(16):5112-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11955059 11955059]
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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=1kx2 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: Shewanella putrefaciens]]
[[Category: Shewanella putrefaciens]]
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[[Category: Single protein]]
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[[Category: Bartalesi I]]
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[[Category: Bartalesi, I.]]
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[[Category: Bertini I]]
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[[Category: Bertini, I.]]
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[[Category: Hajieva P]]
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[[Category: Hajieva, P.]]
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[[Category: Rosato A]]
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[[Category: Rosato, A.]]
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[[Category: Vasos PR]]
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[[Category: Vasos, P R.]]
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[[Category: HEC]]
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[[Category: all-alpha]]
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[[Category: bacteria]]
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[[Category: electron transport]]
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[[Category: ferrocytochrome]]
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[[Category: gram negative]]
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[[Category: haem protein]]
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[[Category: mono haem]]
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[[Category: scya shewanella putrefacien]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:23:19 2008''
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Current revision

Minimized average structure of a mono-heme ferrocytochrome c from Shewanella putrefaciens

PDB ID 1kx2

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