1fi3: Difference between revisions

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-[[Image:1fi3.gif|left|200px]]
-<!--
+==SOLUTION STRUCTURE OF THE M61H MUTANT OF PSEUDOMONAS STUTZERI SUBSTRAIN ZOBELL FERROCYTOCHROME C-551==
-The line below this paragraph, containing "STRUCTURE_1fi3", creates the "Structure Box" on the page.
+<StructureSection load='1fi3' size='340' side='right'caption='[[1fi3]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<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>
-or leave the SCENE parameter empty for the default display.
+</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>
-{{STRUCTURE_1fi3|  PDB=1fi3  |  SCENE=  }}
+<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>
-'''SOLUTION STRUCTURE OF THE M61H MUTANT OF PSEUDOMONAS STUTZERI SUBSTRAIN ZOBELL FERROCYTOCHROME C-551'''
+==See Also==
+*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-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.
+[[Category: Large Structures]]
+[[Category: Pseudomonas stutzeri ATCC 14405 = CCUG 16156]]
-==About this Structure==
+[[Category: Hardman JK]]
-FI3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_stutzeri Pseudomonas stutzeri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FI3 OCA].
+[[Category: Miller GT]]
+[[Category: Timkovich R]]
-==Reference==
-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://www.ncbi.nlm.nih.gov/pubmed/11371465 11371465]
-[[Category: Pseudomonas stutzeri]]
-[[Category: Single protein]]
-[[Category: Hardman, J K.]]
-[[Category: Miller, G T.]]
-[[Category: Timkovich, R.]]
-[[Category: C-551 family]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:21:05 2008''