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| {{STRUCTURE_1doi| PDB=1doi | SCENE= }} | | {{STRUCTURE_1doi| PDB=1doi | SCENE= }} |
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| '''2FE-2S FERREDOXIN FROM HALOARCULA MARISMORTUI'''
| | ===2FE-2S FERREDOXIN FROM HALOARCULA MARISMORTUI=== |
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| ==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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_8612076}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 8612076 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_8612076}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Iron-sulfur]] | | [[Category: Iron-sulfur]] |
| [[Category: Redox protein]] | | [[Category: Redox protein]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:05:16 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:22:47 2008'' |