1DOI
2FE-2S FERREDOXIN FROM HALOARCULA MARISMORTUI
Summary for 1DOI
| Entry DOI | 10.2210/pdb1doi/pdb |
| Descriptor | 2FE-2S FERREDOXIN, POTASSIUM ION, FE2/S2 (INORGANIC) CLUSTER, ... (4 entities in total) |
| Functional Keywords | halophilic protein, redox protein, iron-sulfur, electron transport |
| Biological source | Haloarcula marismortui |
| Total number of polymer chains | 1 |
| Total formula weight | 14823.96 |
| Authors | Frolow, F.,Harel, M.,Sussman, J.L.,Shoham, M. (deposition date: 1996-04-08, release date: 1996-08-01, Last modification date: 2024-02-07) |
| Primary citation | 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 Cited by 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: 8612076DOI: 10.1038/nsb0596-452 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
Download full validation report
