1fhb: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1fhb.jpg|left|200px]]<br /><applet load="1fhb" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1fhb" />
-'''THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE CYANIDE ADDUCT OF A MET80ALA VARIANT OF SACCHAROMYCES CEREVISIAE ISO-1-CYTOCHROME C. IDENTIFICATION OF LIGAND-RESIDUE INTERACTIONS IN THE DISTAL HEME CAVITY'''<br />
-==Overview==
+==THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE CYANIDE ADDUCT OF A MET80ALA VARIANT OF SACCHAROMYCES CEREVISIAE ISO-1-CYTOCHROME C. IDENTIFICATION OF LIGAND-RESIDUE INTERACTIONS IN THE DISTAL HEME CAVITY==
-The 1H NMR spectrum of the the cyanide adduct of a triply mutated, Saccharomyces cerevisiae iso-1-cytochrome c (His39Gln/Met80Ala/Cys102Ser), in the oxidized form has been assigned through 1D NOE and 2D COSY, TOCSY, NOESY, and NOE-NOESY experiments; 562 protons out of a total of 683 have, been assigned. The solution structure, the first of a paramagnetic heme, protein, was determined using 1426 meaningful NOE constraints out of a, total of 1842 measured NOEs. The RMSD values at the stage of restrained, energy minimization of 17 structures obtained from distance geometry, calculations are 0.68 +/- 0.11 and 1.32 +/- 0.14 A for the backbone and, all heavy atoms, respectively. The quality, in terms of RMSD, of the, present structure is the same as that obtained for the solution structure, of the diamagnetic horse heart ferrocytochrome c [Qi, P. X., et al. (1994), Biochemistry 33, 6408-6419]. The secondary structure elements and the, overall folding in the variant are observed to be the same as those of the, wild-type protein for which the X-ray structure is available. However, the, replacement of the methionine axial ligand with an alanine residue creates, a ligand-binding "distal cavity". The properties of the distal cavity seen, in this solution structure are compared to those of other heme proteins.
+<StructureSection load='1fhb' size='340' side='right'caption='[[1fhb]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1fhb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FHB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FHB 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=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</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=1fhb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fhb OCA], [https://pdbe.org/1fhb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fhb RCSB], [https://www.ebi.ac.uk/pdbsum/1fhb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fhb ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CYC1_YEAST CYC1_YEAST] Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
+== 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/fh/1fhb_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=1fhb ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-FHB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with CYN, HEM and TML as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FHB OCA].
+*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-Three-dimensional solution structure of the cyanide adduct of a Met80Ala variant of Saccharomyces cerevisiae iso-1-cytochrome c. Identification of ligand-residue interactions in the distal heme cavity., Banci L, Bertini I, Bren KL, Gray HB, Sompornpisut P, Turano P, Biochemistry. 1995 Sep 12;34(36):11385-98. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7547866 7547866]
+[[Category: Large Structures]]
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Single protein]]
+[[Category: Banci L]]
-[[Category: Banci, L.]]
+[[Category: Bertini I]]
-[[Category: Bertini, I.]]
+[[Category: Bren KL]]
-[[Category: Bren, K.L.]]
+[[Category: Gray HB]]
-[[Category: Gray, H.B.]]
+[[Category: Sompornpisut P]]
-[[Category: Sompornpisut, P.]]
+[[Category: Turano P]]
-[[Category: Turano, P.]]
-[[Category: CYN]]
-[[Category: HEM]]
-[[Category: TML]]
-[[Category: electron transport]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:55:25 2007''