1doi
From Proteopedia
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| - | [[Image:1doi.gif|left|200px]]<br /> | + | [[Image:1doi.gif|left|200px]]<br /><applet load="1doi" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1doi" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1doi, resolution 1.9Å" /> | caption="1doi, resolution 1.9Å" /> | ||
'''2FE-2S FERREDOXIN FROM HALOARCULA MARISMORTUI'''<br /> | '''2FE-2S FERREDOXIN FROM HALOARCULA MARISMORTUI'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 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]. | + | 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]. Known structural/functional Site: <scene name='pdbsite=22:Fe2s2 Fe-S Redox Center'>22</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DOI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: redox protein]] | [[Category: redox protein]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 14:44:48 2007'' |
Revision as of 12:35, 18 December 2007
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2FE-2S FERREDOXIN FROM HALOARCULA MARISMORTUI
Overview
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
1DOI is a Single protein structure of sequence from Haloarcula marismortui with K and FES as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
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
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