1doi
From Proteopedia
| Line 5: | Line 5: | ||
==Overview== | ==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 . | + | 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== | ==About this Structure== | ||
| - | 1DOI is a | + | 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]. |
==Reference== | ==Reference== | ||
| Line 25: | Line 25: | ||
[[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 Mon Nov 5 14:55:10 2007'' |
Revision as of 12:49, 5 November 2007
|
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. Structure known Active Site: 22. 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
Page seeded by OCA on Mon Nov 5 14:55:10 2007
