1doi

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[[Image:1doi.gif|left|200px]]
 
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{{Structure
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==2FE-2S FERREDOXIN FROM HALOARCULA MARISMORTUI==
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|PDB= 1doi |SIZE=350|CAPTION= <scene name='initialview01'>1doi</scene>, resolution 1.9&Aring;
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<StructureSection load='1doi' size='340' side='right'caption='[[1doi]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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|SITE= <scene name='pdbsite=22:Fe2s2+Fe-S+Redox+Center'>22</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>
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<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>
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|ACTIVITY=
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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]] 1.9&#8491;</td></tr>
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|GENE=
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<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>
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|DOMAIN=
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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=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>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1doi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1doi OCA], [http://www.ebi.ac.uk/pdbsum/1doi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1doi RCSB]</span>
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== Function ==
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[https://www.uniprot.org/uniprot/FER1_HALMA FER1_HALMA] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
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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/do/1doi_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=1doi ConSurf].
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<div style="clear:both"></div>
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'''2FE-2S FERREDOXIN FROM HALOARCULA MARISMORTUI'''
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==See Also==
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*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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==About this Structure==
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1DOI is a [[Single protein]] structure of sequence from [http://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].
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==Reference==
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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://www.ncbi.nlm.nih.gov/pubmed/8612076 8612076]
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[[Category: Haloarcula marismortui]]
[[Category: Haloarcula marismortui]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Frolow, F.]]
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[[Category: Frolow F]]
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[[Category: Harel, M.]]
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[[Category: Harel M]]
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[[Category: Shoham, M.]]
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[[Category: Shoham M]]
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[[Category: Sussman, J L.]]
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[[Category: Sussman JL]]
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[[Category: electron transport]]
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[[Category: halophilic protein]]
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[[Category: iron-sulfur]]
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[[Category: redox protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:45:31 2008''
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Current revision

2FE-2S FERREDOXIN FROM HALOARCULA MARISMORTUI

PDB ID 1doi

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