PDBsum entry 1doi

Electron transport

PDB id: 1doi

Contents

Protein chain

128 a.a.

Ligands

FES

Metals

__K ×6

Waters ×237

References listed in PDB file

Key reference

• Title: Insights into protein adaptation to a saturated salt environment from the crystal structure of a halophilic 2fe-2s ferredoxin.
• Authors: F.Frolow, M.Harel, J.L.Sussman, M.Mevarech, M.Shoham.
• Ref.: Nat Struct Biol, 1996, 3, 452-458.
• PubMed id: 8612076

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.

Secondary reference #1

• Title: X-Ray structural studies of a salt-Loving 2fe-2s ferredoxin from halobacterium of the dead sea
• Authors: J.L.Sussman, J.H.Brown, M.Shoham.
• Ref.: iron-sulfur protein research ...

Secondary reference #2

• Title: Preliminary X-Ray diffraction studies on 2 fe-Ferredoxin from halobacterium of the dead sea.
• Authors: J.L.Sussman, P.Zipori, M.Harel, A.Yonath, M.M.Werber.
• Ref.: J Mol Biol, 1979, 134, 375-377.
• PubMed id: 537068