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< | ==Solution Conformation of the H47A Mutant of Pseudomonas stutzeri ZoBell Ferrocytochrome c-551== | ||
<StructureSection load='2i8f' size='340' side='right'caption='[[2i8f]]' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2i8f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_stutzeri_ATCC_14405_=_CCUG_16156 Pseudomonas stutzeri ATCC 14405 = CCUG 16156]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I8F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I8F FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</td></tr> | |||
-- | <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> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2i8f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i8f OCA], [https://pdbe.org/2i8f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i8f RCSB], [https://www.ebi.ac.uk/pdbsum/2i8f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i8f ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CY551_STUST CY551_STUST] Electron donor for cytochrome cd1 in nitrite and nitrate respiration. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<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/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=2i8f ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In 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<ref>PMID:17496029</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2i8f" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
[[Category: Pseudomonas stutzeri ATCC 14405 = CCUG 16156]] | |||
[[Category: Liang Q]] | |||
== | [[Category: Timkovich R]] | ||
[[Category: | |||
[[Category: | |||
[[Category: Liang | |||
[[Category: Timkovich | |||
Latest revision as of 04:03, 21 November 2024
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
FunctionCY551_STUST 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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