1doi: Difference between revisions

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-[[Image:1doi.gif|left|200px]]<br />
-<applet load="1doi" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1doi, resolution 1.9&Aring;" />
-'''2FE-2S FERREDOXIN FROM HALOARCULA MARISMORTUI'''<br />
-==Overview==
+==2FE-2S FERREDOXIN FROM HALOARCULA MARISMORTUI==
-Haloarcula marismortui is an archaebacterium that flourishes in the, world's saltiest body of water, the Dead Sea. The cytosol of this organism, is a supersaturated salt solution in which proteins are soluble and, active. The crystal structure of a 2Fe-2S ferredoxin from H. marismortui, determined at 1.9 A is similar to those of plant-type 2Fe-2S ferredoxins, of known structure, with two important distinctions. The entire surface of, the protein is coated with acidic residues except for the vicinity of the, iron-sulphur cluster, and there is an insertion of two amphipathic helices, near the N-terminus. These form a separate hyperacidic domain whose, postulated function to provide extra surface carboxylates for solvation., These data and the fact that bound surface water molecules have on the, average 40% more hydrogen bonds than in a typical non-halophilic protein, crystal structure support the notion that haloadaptation involves better, water binding capacity.
+<StructureSection load='1doi' size='340' side='right'caption='[[1doi]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1doi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haloarcula_marismortui Haloarcula marismortui]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DOI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DOI FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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=1doi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1doi OCA], [https://pdbe.org/1doi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1doi RCSB], [https://www.ebi.ac.uk/pdbsum/1doi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1doi ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/FER1_HALMA FER1_HALMA] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
+== 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/do/1doi_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=1doi ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-DOI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haloarcula_marismortui Haloarcula marismortui] with K and FES as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: 22. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DOI OCA].
+*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-Insights into protein adaptation to a saturated salt environment from the crystal structure of a halophilic 2Fe-2S ferredoxin., Frolow F, Harel M, Sussman JL, Mevarech M, Shoham M, Nat Struct Biol. 1996 May;3(5):452-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8612076 8612076]
 [[Category: Haloarcula marismortui]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Frolow, F.]]
+[[Category: Frolow F]]
-[[Category: Harel, M.]]
+[[Category: Harel M]]
-[[Category: Shoham, M.]]
+[[Category: Shoham M]]
-[[Category: Sussman, J.L.]]
+[[Category: Sussman JL]]
-[[Category: FES]]
-[[Category: K]]
-[[Category: electron transport]]
-[[Category: halophilic protein]]
-[[Category: iron-sulfur]]
-[[Category: redox protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov  5 16:01:21 2007''