1doi
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Haloarcula marismortui is an archaebacterium that flourishes in the | + | 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== | ||
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[[Category: Harel, M.]] | [[Category: Harel, M.]] | ||
[[Category: Shoham, M.]] | [[Category: Shoham, M.]] | ||
| - | [[Category: Sussman, J | + | [[Category: Sussman, J L.]] |
[[Category: FES]] | [[Category: FES]] | ||
[[Category: K]] | [[Category: K]] | ||
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[[Category: redox protein]] | [[Category: redox protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:18:51 2008'' |
Revision as of 10:18, 21 February 2008
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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 and 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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