1fi3: Difference between revisions

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OCA

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-[[Image:1fi3.gif|left|200px]]<br /><applet load="1fi3" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1fi3" />
-'''SOLUTION STRUCTURE OF THE M61H MUTANT OF PSEUDOMONAS STUTZERI SUBSTRAIN ZOBELL FERROCYTOCHROME C-551'''<br />
-==Overview==
+==SOLUTION STRUCTURE OF THE M61H MUTANT OF PSEUDOMONAS STUTZERI SUBSTRAIN ZOBELL FERROCYTOCHROME C-551==
-The gene encoding for bacterial cytochrome c-551 from Pseudomonas stutzeri, substrain ZoBell has been mutated to convert the invariant sixth ligand, methionine residue into histidine, creating the site-specific mutant M61H., Proton NMR resonance assignments were made for all main-chain and, most-side chain protons in the diamagnetic, reduced form at pH 9.2 and 333, K by two-dimensional NMR techniques. Distance constraints (1074) were, determined from nuclear Overhauser enhancements and main-chain, torsion-angle constraints (72) from scalar coupling estimates. Solution, conformations for the protein were computed by the simulated annealing, approach. For 28 computed structures, the root mean squared displacement, from the average structure excluding the terminal residues 1, 2, 81, and, 82 was 0.52 A (sigma = 0.096) for backbone atoms and 0.90 A (sigma =, 0.122) for all heavy atoms. The global folding of the mutant protein is, the same as for wild type. The biggest changes are localized in a peptide, span over residues 60-65. The most striking behavior of the mutant protein, is that at room temperature and neutral pH it exists in a state similar to, the molten globular state that has been described for several proteins, under mild denaturing conditions, but the mutant converts to a more, ordered state at high pH and temperature.
+<StructureSection load='1fi3' size='340' side='right'caption='[[1fi3]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1fi3]] 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=1FI3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FI3 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1fi3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fi3 OCA], [https://pdbe.org/1fi3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fi3 RCSB], [https://www.ebi.ac.uk/pdbsum/1fi3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fi3 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/fi/1fi3_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1fi3 ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-FI3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_stutzeri Pseudomonas stutzeri] with HEC as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FI3 OCA].
+*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-Solution conformation of the Met 61 to His 61 mutant of Pseudomonas stutzeri ZoBell ferrocytochrome c-551., Miller GT, Hardman JK, Timkovich R, Biophys J. 2001 Jun;80(6):2928-34. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11371465 11371465]
+[[Category: Large Structures]]
-[[Category: Pseudomonas stutzeri]]
+[[Category: Pseudomonas stutzeri ATCC 14405 = CCUG 16156]]
-[[Category: Single protein]]
+[[Category: Hardman JK]]
-[[Category: Hardman, J.K.]]
+[[Category: Miller GT]]
-[[Category: Miller, G.T.]]
+[[Category: Timkovich R]]
-[[Category: Timkovich, R.]]
-[[Category: HEC]]
-[[Category: c-551 family]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:56:23 2007''