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1doi

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==Overview==
==Overview==
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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.
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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.]]
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[[Category: Sussman, J.L.]]
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[[Category: Sussman, J L.]]
[[Category: FES]]
[[Category: FES]]
[[Category: K]]
[[Category: K]]
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[[Category: redox protein]]
[[Category: redox protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:35:35 2008''
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''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


1doi, resolution 1.9Å

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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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