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1lm2

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Revision as of 07:52, 31 January 2018

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

Structural highlights

1lm2 is a 1 chain structure with sequence from Desulfuromonas acetoxidans. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1new, 2new, 1ehj, 1hh5
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CYC3_DESAC] Participates in sulfate respiration coupled with phosphorylation by transferring electrons from the enzyme dehydrogenase to ferredoxin.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Assfalg M, Bertini I, Bruschi M, Michel C, Turano P. 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). Proc Natl Acad Sci U S A. 2002 Jul 23;99(15):9750-4. Epub 2002 Jul 15. PMID:12119407 doi:10.1073/pnas.152290999

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1lm2"

@@ Line 1: / Line 1: @@
 ==NMR structural characterization of the reduction of chromium(VI) to chromium(III) by cytochrome c7==
 <StructureSection load='1lm2' size='340' side='right' caption='[[1lm2]], [[NMR_Ensembles_of_Models | 35 NMR models]]' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CR:CHROMIUM+ION'>CR</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1new|1new]], [[2new|2new]], [[1ehj|1ehj]], [[1hh5|1hh5]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lm2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lm2 OCA], [http://pdbe.org/1lm2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lm2 RCSB], [http://www.ebi.ac.uk/pdbsum/1lm2 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lm2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lm2 OCA], [http://pdbe.org/1lm2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lm2 RCSB], [http://www.ebi.ac.uk/pdbsum/1lm2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lm2 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lm/1lm2_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lm/1lm2_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 30: / Line 31: @@
 ==See Also==
-*[[Cytochrome c|Cytochrome c]]
 *[[Cytochrome c 7|Cytochrome c 7]]
 == References ==

1lm2

From Proteopedia

Revision as of 07:52, 31 January 2018

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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