1doi
From Proteopedia
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|PDB= 1doi |SIZE=350|CAPTION= <scene name='initialview01'>1doi</scene>, resolution 1.9Å | |PDB= 1doi |SIZE=350|CAPTION= <scene name='initialview01'>1doi</scene>, resolution 1.9Å | ||
|SITE= <scene name='pdbsite=22:Fe2s2+Fe-S+Redox+Center'>22</scene> | |SITE= <scene name='pdbsite=22:Fe2s2+Fe-S+Redox+Center'>22</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1doi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1doi OCA], [http://www.ebi.ac.uk/pdbsum/1doi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1doi RCSB]</span> | ||
}} | }} | ||
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[[Category: Shoham, M.]] | [[Category: Shoham, M.]] | ||
[[Category: Sussman, J L.]] | [[Category: Sussman, J L.]] | ||
| - | [[Category: FES]] | ||
| - | [[Category: K]] | ||
[[Category: electron transport]] | [[Category: electron transport]] | ||
[[Category: halophilic protein]] | [[Category: halophilic protein]] | ||
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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 Sun Mar 30 19:45:31 2008'' |
Revision as of 16:45, 30 March 2008
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| , resolution 1.9Å | |||||||
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| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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