2i8f: Difference between revisions
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==Solution Conformation of the H47A Mutant of Pseudomonas stutzeri ZoBell Ferrocytochrome c-551== | ==Solution Conformation of the H47A Mutant of Pseudomonas stutzeri ZoBell Ferrocytochrome c-551== | ||
<StructureSection load='2i8f' size='340' side='right' caption='[[2i8f]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | <StructureSection load='2i8f' size='340' side='right' caption='[[2i8f]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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">[[1cch|1cch]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1cch|1cch]]</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=2i8f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i8f OCA], [http://pdbe.org/2i8f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2i8f RCSB], [http://www.ebi.ac.uk/pdbsum/2i8f 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=2i8f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i8f OCA], [http://pdbe.org/2i8f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2i8f RCSB], [http://www.ebi.ac.uk/pdbsum/2i8f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2i8f ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i8/2i8f_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i8/2i8f_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 11:39, 4 July 2018
Solution Conformation of the H47A Mutant of Pseudomonas stutzeri ZoBell Ferrocytochrome c-551Solution Conformation of the H47A Mutant of Pseudomonas stutzeri ZoBell Ferrocytochrome c-551
Structural highlights
Function[CY551_PSEST] Electron donor for cytochrome cd1 in nitrite and nitrate respiration. 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 PubMedIn the cytochrome c-551 family, the heme 17-propionate caboxylate group is always hydrogen bonded to an invariant Trp-56 and conserved residues (His and Arg mainly, Lys occasionally) at position 47. The mutation of His-47 to Ala-47 for Pseudomas stutzeri ZoBell cytochrome c-551 removes this otherwise invariant hydrogen bond. The solution structure of ferrous H47A has been solved based on NMR-derived constraints. Results indicate that the mutant has very similar main chain folding compared to wild-type. However, less efficient packing of residues in the mutant surrounding the heme propionates leads to more solvent exposure for both propionate groups, which may account for decreased stability of the mutant. The mutant has a reduction potential different from wild-type, and furthermore, the pH dependence of this potential is not the same as for wild-type. The structure of the mutant suggests that these changes are related to the loss of the residue-47 propionate hydrogen bond and the loss of charge on the side chain of residue 47. Solution conformation of the His-47 to Ala-47 mutant of Pseudomonas stutzeri ZoBell ferrocytochrome c-551.,Liang Q, Miller GT, Beeghley CA, Graf CB, Timkovich R Biophys J. 2007 Sep 1;93(5):1700-6. Epub 2007 May 11. PMID:17496029[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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