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1i6e

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(New page: 200px<br /><applet load="1i6e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i6e" /> '''SOLUTION STRUCTURE OF THE FUNCTIONAL DOMAIN ...)
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[[Image:1i6e.jpg|left|200px]]<br /><applet load="1i6e" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1i6e" />
 
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'''SOLUTION STRUCTURE OF THE FUNCTIONAL DOMAIN OF PARACOCCUS DENITRIFICANS CYTOCHROME C552 IN THE OXIDIZED STATE'''<br />
 
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==Overview==
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==SOLUTION STRUCTURE OF THE FUNCTIONAL DOMAIN OF PARACOCCUS DENITRIFICANS CYTOCHROME C552 IN THE OXIDIZED STATE==
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A soluble and fully functional 10.5 kDa fragment of the 18.2 kDa, membrane-bound cytochrome c(552) from Paracoccus denitrificans has been, heterologously expressed and (13)C/(15)N-labeled to study the structural, features of this protein in both redox states. Well-resolved solution, structures of both the reduced and oxidized states have been determined, using high-resolution heteronuclear NMR. The overall protein topology, consists of two long terminal helices and three shorter helices, surrounding the heme moiety. No significant redox-induced structural, differences have been observed. (15)N relaxation rates and heteronuclear, NOE values were determined at 500 and 600 MHz. Several residues located, around the heme moiety display increased backbone mobility in both, oxidation states, while helices I, III, and V as well as the two, concatenated beta-turns between Leu30 and Arg36 apparently form a less, flexible domain within the protein structure. Major redox-state-dependent, differences of the internal backbone mobility on the picosecond-nanosecond, time scale were not evident. Hydrogen exchange experiments demonstrated, that the slow-exchanging amide proton resonances mainly belong to the, helices and beta-turns, corresponding to the regions with high order, parameters in the dynamics data. Despite this correlation, the backbone, amide protons of the oxidized cytochrome c(552) exchange considerably, faster with the solvent compared to the reduced protein. Using both, differential scanning calorimetry as well as temperature-dependent NMR, spectroscopy, a significant difference in the thermostabilities of the two, redox states has been observed, with transition temperatures of 349.9 K, (76.8 degrees C) for reduced and 307.5 K (34.4 degrees C) for oxidized, cytochrome c(552). These results suggest a clearly distinct backbone, stability between the two oxidation states.
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<StructureSection load='1i6e' size='340' side='right'caption='[[1i6e]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1i6e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I6E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I6E 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">Solution NMR</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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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1i6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i6e OCA], [https://pdbe.org/1i6e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i6e RCSB], [https://www.ebi.ac.uk/pdbsum/1i6e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i6e ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CY552_PARDE CY552_PARDE]
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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/i6/1i6e_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=1i6e 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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1I6E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans] with HEC as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1I6E OCA].
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*[[Cytochrome c nitrite reductase|Cytochrome c nitrite reductase]]
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__TOC__
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==Reference==
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</StructureSection>
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Solution structure and dynamics of the functional domain of Paracoccus denitrificans cytochrome c(552) in both redox states., Reincke B, Perez C, Pristovsek P, Lucke C, Ludwig C, Lohr F, Rogov VV, Ludwig B, Ruterjans H, Biochemistry. 2001 Oct 16;40(41):12312-20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11591150 11591150]
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[[Category: Large Structures]]
[[Category: Paracoccus denitrificans]]
[[Category: Paracoccus denitrificans]]
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[[Category: Single protein]]
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[[Category: Loehr F]]
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[[Category: Loehr, F.]]
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[[Category: Ludwig B]]
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[[Category: Ludwig, B.]]
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[[Category: Ludwig C]]
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[[Category: Ludwig, C.]]
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[[Category: Luecke C]]
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[[Category: Luecke, C.]]
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[[Category: Perez C]]
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[[Category: Perez, C.]]
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[[Category: Pristovsek P]]
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[[Category: Pristovsek, P.]]
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[[Category: Reincke B]]
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[[Category: Reincke, B.]]
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[[Category: Rogov VV]]
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[[Category: Rogov, V.V.]]
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[[Category: Rueterjans H]]
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[[Category: Rueterjans, H.]]
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[[Category: HEC]]
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[[Category: cytochrome c552]]
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[[Category: electron transport]]
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[[Category: heme]]
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[[Category: isotope enrichment {13c/15n}]]
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[[Category: nmr spectroscopy]]
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[[Category: redox states]]
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[[Category: solution structure]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:05:24 2007''
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Current revision

SOLUTION STRUCTURE OF THE FUNCTIONAL DOMAIN OF PARACOCCUS DENITRIFICANS CYTOCHROME C552 IN THE OXIDIZED STATE

PDB ID 1i6e

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