1doi: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1doi]] is a 1 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DOI FirstGlance]. <br> | <table><tr><td colspan='2'>[[1doi]] is a 1 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DOI FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1doi RCSB], [http://www.ebi.ac.uk/pdbsum/1doi PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1doi RCSB], [http://www.ebi.ac.uk/pdbsum/1doi PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Haloarcula marismortui]] | [[Category: Haloarcula marismortui]] | ||
[[Category: Frolow, F | [[Category: Frolow, F]] | ||
[[Category: Harel, M | [[Category: Harel, M]] | ||
[[Category: Shoham, M | [[Category: Shoham, M]] | ||
[[Category: Sussman, J L | [[Category: Sussman, J L]] | ||
[[Category: Electron transport]] | [[Category: Electron transport]] | ||
[[Category: Halophilic protein]] | [[Category: Halophilic protein]] | ||
[[Category: Iron-sulfur]] | [[Category: Iron-sulfur]] | ||
[[Category: Redox protein]] | [[Category: Redox protein]] | ||
Revision as of 07:39, 24 November 2014
2FE-2S FERREDOXIN FROM HALOARCULA MARISMORTUI2FE-2S FERREDOXIN FROM HALOARCULA MARISMORTUI
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHaloarcula 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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