1DOI

2FE-2S FERREDOXIN FROM HALOARCULA MARISMORTUI

1DOI の概要

• エントリーDOI: 10.2210/pdb1doi/pdb
• 分子名称: 2FE-2S FERREDOXIN, POTASSIUM ION, FE2/S2 (INORGANIC) CLUSTER, ... (4 entities in total)
• 機能のキーワード: halophilic protein, redox protein, iron-sulfur, electron transport
• 由来する生物種: Haloarcula marismortui
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14823.96

構造登録者

Frolow, F.,Harel, M.,Sussman, J.L.,Shoham, M. (登録日: 1996-04-08, 公開日: 1996-08-01, 最終更新日: 2024-02-07)

主引用文献

Frolow, F.,Harel, M.,Sussman, J.L.,Mevarech, M.,Shoham, M.
Insights into protein adaptation to a saturated salt environment from the crystal structure of a halophilic 2Fe-2S ferredoxin.
Nat.Struct.Biol., 3:452-458, 1996

PubMed Abstract: 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.

PubMed: 8612076
DOI: 10.1038/nsb0596-452

実験手法

X-RAY DIFFRACTION (1.9 Å)