1k3g

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[[Image:1k3g.jpg|left|200px]]
 
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==NMR Solution Structure of Oxidized Cytochrome c-553 from Bacillus pasteurii==
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The line below this paragraph, containing "STRUCTURE_1k3g", creates the "Structure Box" on the page.
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<StructureSection load='1k3g' size='340' side='right'caption='[[1k3g]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1k3g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sporosarcina_pasteurii Sporosarcina pasteurii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K3G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K3G FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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, 30 models</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></td></tr>
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{{STRUCTURE_1k3g| PDB=1k3g | SCENE= }}
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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=1k3g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k3g OCA], [https://pdbe.org/1k3g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k3g RCSB], [https://www.ebi.ac.uk/pdbsum/1k3g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k3g ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CY553_SPOPA CY553_SPOPA]
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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/k3/1k3g_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1k3g ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The solution structure of oxidized cytochrome c(553) (71 amino acid residues) from the Gram-positive bacterium Bacillus pasteurii is here reported and compared with the available crystal structure. The solution structure is obtained from 1609 meaningful NOE data (22.7 per residue), 76 dihedral angles, and 59 pseudocontact shifts. The root mean square deviations from the average structure are 0.25+/-0.07 and 0.59+/-0.13 A for the backbone and all heavy atoms, respectively, and the quality assessment of the structure is satisfactory. The solution structure closely reproduces the fold observed in the crystal structure. The backbone mobility was then investigated through amide (15)N relaxation rate and (15)N-(1)H NOE measurements. The protein is rigid in both the sub-nanosecond and millisecond time scales, probably due to the relatively large heme:number of amino acids ratio. Modeling of eight c-type cytochromes from other Gram-positive bacteria with a high sequence identity (&gt;30 %) to the present cytochrome c(553) was performed. Analysis of consensus features accounts for the relatively low reduction potential as being due to extensive heme hydration and indicates residues 34-35, 44-46, 69-72, and 75 as a conserved hydrophobic patch for the interaction with a protein partner. At variance with mitochondrial c-type cytochrome, this protein does not experience pH-dependent coordination equilibria. The reasons for this difference are analyzed.
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'''NMR Solution Structure of Oxidized Cytochrome c-553 from Bacillus pasteurii'''
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NMR solution structure, backbone mobility, and homology modeling of c-type cytochromes from gram-positive bacteria.,Banci L, Bertini I, Ciurli S, Dikiy A, Dittmer J, Rosato A, Sciara G, Thompsett AR Chembiochem. 2002 Apr 2;3(4):299-310. PMID:11933230<ref>PMID:11933230</ref>
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==Overview==
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The solution structure of oxidized cytochrome c(553) (71 amino acid residues) from the Gram-positive bacterium Bacillus pasteurii is here reported and compared with the available crystal structure. The solution structure is obtained from 1609 meaningful NOE data (22.7 per residue), 76 dihedral angles, and 59 pseudocontact shifts. The root mean square deviations from the average structure are 0.25+/-0.07 and 0.59+/-0.13 A for the backbone and all heavy atoms, respectively, and the quality assessment of the structure is satisfactory. The solution structure closely reproduces the fold observed in the crystal structure. The backbone mobility was then investigated through amide (15)N relaxation rate and (15)N-(1)H NOE measurements. The protein is rigid in both the sub-nanosecond and millisecond time scales, probably due to the relatively large heme:number of amino acids ratio. Modeling of eight c-type cytochromes from other Gram-positive bacteria with a high sequence identity (&gt;30 %) to the present cytochrome c(553) was performed. Analysis of consensus features accounts for the relatively low reduction potential as being due to extensive heme hydration and indicates residues 34-35, 44-46, 69-72, and 75 as a conserved hydrophobic patch for the interaction with a protein partner. At variance with mitochondrial c-type cytochrome, this protein does not experience pH-dependent coordination equilibria. The reasons for this difference are analyzed.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1K3G is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sporosarcina_pasteurii Sporosarcina pasteurii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K3G OCA].
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</div>
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<div class="pdbe-citations 1k3g" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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NMR solution structure, backbone mobility, and homology modeling of c-type cytochromes from gram-positive bacteria., Banci L, Bertini I, Ciurli S, Dikiy A, Dittmer J, Rosato A, Sciara G, Thompsett AR, Chembiochem. 2002 Apr 2;3(4):299-310. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11933230 11933230]
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*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
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[[Category: Single protein]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Sporosarcina pasteurii]]
[[Category: Sporosarcina pasteurii]]
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[[Category: Banci, L.]]
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[[Category: Banci L]]
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[[Category: Bertini, I.]]
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[[Category: Bertini I]]
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[[Category: Ciurli, S.]]
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[[Category: Ciurli S]]
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[[Category: Dikiy, A.]]
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[[Category: Dikiy A]]
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[[Category: Dittmer, J.]]
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[[Category: Dittmer J]]
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[[Category: Rosato, A.]]
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[[Category: Rosato A]]
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[[Category: Sciara, G.]]
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[[Category: Sciara G]]
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[[Category: Thompsett, A R.]]
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[[Category: Thompsett AR]]
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[[Category: Bacillus pasteurii]]
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[[Category: C-553]]
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[[Category: Cytochrome]]
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[[Category: Electron transfer]]
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[[Category: Heme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:15:22 2008''
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Current revision

NMR Solution Structure of Oxidized Cytochrome c-553 from Bacillus pasteurii

PDB ID 1k3g

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