1lm2

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{{Seed}}
 
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[[Image:1lm2.png|left|200px]]
 
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==NMR structural characterization of the reduction of chromium(VI) to chromium(III) by cytochrome c7==
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The line below this paragraph, containing "STRUCTURE_1lm2", creates the "Structure Box" on the page.
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<StructureSection load='1lm2' size='340' side='right'caption='[[1lm2]]' 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'>[[1lm2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfuromonas_acetoxidans Desulfuromonas acetoxidans]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LM2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LM2 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, 35 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=CR:CHROMIUM+ION'>CR</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
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{{STRUCTURE_1lm2| PDB=1lm2 | 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=1lm2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lm2 OCA], [https://pdbe.org/1lm2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lm2 RCSB], [https://www.ebi.ac.uk/pdbsum/1lm2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lm2 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CYC3_DESAC CYC3_DESAC] Participates in sulfate respiration coupled with phosphorylation by transferring electrons from the enzyme dehydrogenase to ferredoxin.
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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/lm/1lm2_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=1lm2 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 redox reaction between CrO(4)(2-) and the fully reduced three-heme cytochrome c(7) from Desulfuromonas acetoxidans to give chromium(III) and the fully oxidized protein has been followed by NMR spectroscopy. The hyperfine coupling between the oxidized protein protons and chromium(III), which remains bound to the protein, gives rise to line-broadening effects on the NMR resonances that can be transformed into proton-metal distance restraints. Structure calculations based on these unconventional constraints allowed us to demonstrate that chromium(III) binds at a unique site and to locate it on the protein surface. The metal ion is located 7.9 +/- 0.4 A from the iron of heme IV, 16.3 +/- 0.7 A from the iron of heme III, and 22.5 +/- 0.5 A from the iron of heme I. Shift changes caused by the presence of unreactive MoO(4)(2-), a CrO(4)(2-) analogue, indicate the involvement of the same protein area in the anion binding. The titration of the oxidation of cytochrome c(7) shows a detailed mechanism of action. The presence of a specific binding site supports the hypothesis of the biological role of this cytochrome as a metal reductase.
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===NMR structural characterization of the reduction of chromium(VI) to chromium(III) by cytochrome c7===
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The metal reductase activity of some multiheme cytochromes c: NMR structural characterization of the reduction of chromium(VI) to chromium(III) by cytochrome c(7).,Assfalg M, Bertini I, Bruschi M, Michel C, Turano P Proc Natl Acad Sci U S A. 2002 Jul 23;99(15):9750-4. Epub 2002 Jul 15. PMID:12119407<ref>PMID:12119407</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1lm2" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_12119407}}, adds the Publication Abstract to the page
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*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 12119407 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12119407}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1LM2 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Desulfuromonas_acetoxidans Desulfuromonas acetoxidans]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LM2 OCA].
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==Reference==
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<ref group="xtra">PMID:12119407</ref><references group="xtra"/>
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[[Category: Desulfuromonas acetoxidans]]
[[Category: Desulfuromonas acetoxidans]]
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[[Category: Assfalg, M.]]
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[[Category: Large Structures]]
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[[Category: Bertini, I.]]
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[[Category: Assfalg M]]
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[[Category: Bruschi, M.]]
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[[Category: Bertini I]]
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[[Category: Michel, C.]]
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[[Category: Bruschi M]]
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[[Category: Turano, P.]]
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[[Category: Michel C]]
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[[Category: Chromium]]
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[[Category: Turano P]]
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[[Category: Cytochrome c7]]
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[[Category: Nmr]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 10:38:31 2009''
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Current revision

NMR structural characterization of the reduction of chromium(VI) to chromium(III) by cytochrome c7

PDB ID 1lm2

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