1za5

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[[Image:1za5.gif|left|200px]]
 
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==Q69H-FeSOD==
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The line below this paragraph, containing "STRUCTURE_1za5", creates the "Structure Box" on the page.
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<StructureSection load='1za5' size='340' side='right'caption='[[1za5]], [[Resolution|resolution]] 1.80&Aring;' 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'>[[1za5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZA5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZA5 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">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</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=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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{{STRUCTURE_1za5| PDB=1za5 | 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=1za5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1za5 OCA], [https://pdbe.org/1za5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1za5 RCSB], [https://www.ebi.ac.uk/pdbsum/1za5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1za5 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SODF_ECOLI SODF_ECOLI] Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
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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/za/1za5_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=1za5 ConSurf].
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<div style="clear:both"></div>
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'''Q69H-FeSOD'''
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==See Also==
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*[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Fe-containing superoxide dismutase's active site Fe is coordinated by a solvent molecule, whose protonation state is coupled to the Fe oxidation state. Thus, we have proposed that H-bonding between glutamine 69 and this solvent molecule can strongly influence the redox activity of the Fe in superoxide dismutase (SOD). We show here that mutation of this Gln to His subtly alters the active site structure but preserves 30% activity. In contrast, mutation to Glu otherwise preserves the active site structure but inactivates the enzyme. Thus, enzyme function correlates not with atom positions but with residue identity (chemistry), in this case. We observe strong destabilization of the Q69E-FeSOD oxidized state relative to the reduced state and intermediate destabilization of oxidized Q69H-FeSOD. Indeed, redox titrations indicate that mutation of Gln69 to His increases the reduction potential by 240 mV, whereas mutation to Glu appears to increase it by more than 660 mV. We find that this suffices to explain the mutants' loss of activity, although additional factors may also contribute. The strongly elevated reduction potential of Q69E-FeSOD may reflect reorganization of the active site H-bonding network, including possible reversal of the polarity of the key H-bond between residue 69 and coordinated solvent.
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==About this Structure==
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1ZA5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZA5 OCA].
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==Reference==
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The crucial importance of chemistry in the structure-function link: manipulating hydrogen bonding in iron-containing superoxide dismutase., Yikilmaz E, Rodgers DW, Miller AF, Biochemistry. 2006 Jan 31;45(4):1151-61. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16430211 16430211]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Superoxide dismutase]]
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[[Category: Miller AF]]
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[[Category: Miller, A F.]]
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[[Category: Rodgers DW]]
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[[Category: Rodgers, D W.]]
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[[Category: Yikilmaz E]]
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[[Category: Yikilmaz, E.]]
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[[Category: H-bonding redox tuning superoxide dismutase proton-coupled electron transfer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:22:41 2008''
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Current revision

Q69H-FeSOD

PDB ID 1za5

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