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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==
1DOI 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: 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 Thu Nov  8 12:39:12 2007''

Latest revision as of 09:57, 7 February 2024

2FE-2S FERREDOXIN FROM HALOARCULA MARISMORTUI2FE-2S FERREDOXIN FROM HALOARCULA MARISMORTUI

Structural highlights

1doi is a 1 chain structure with sequence from Haloarcula marismortui. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FER1_HALMA Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1doi, resolution 1.90Å

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