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[[Image:1doi.gif|left|200px]]
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{{STRUCTURE_1doi|  PDB=1doi  |  SCENE=  }}
'''2FE-2S FERREDOXIN FROM HALOARCULA MARISMORTUI'''


==2FE-2S FERREDOXIN FROM HALOARCULA MARISMORTUI==
<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/initialview03.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>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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:8612076<ref>PMID:8612076</ref>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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].
</div>
<div class="pdbe-citations 1doi" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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]
*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Haloarcula marismortui]]
[[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: Electron transport]]
[[Category: Halophilic protein]]
[[Category: Iron-sulfur]]
[[Category: Redox protein]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:05:16 2008''
Retrieved from "https://proteopedia.org/1doi"