1aor: Difference between revisions
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[[Image:1aor.gif|left|200px]] | [[Image:1aor.gif|left|200px]] | ||
'''STRUCTURE OF A HYPERTHERMOPHILIC TUNGSTOPTERIN ENZYME, ALDEHYDE FERREDOXIN OXIDOREDUCTASE''' | {{Structure | ||
|PDB= 1aor |SIZE=350|CAPTION= <scene name='initialview01'>1aor</scene>, resolution 2.3Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene> and <scene name='pdbligand=PTE:TUNGSTOPTERIN COFACTOR'>PTE</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''STRUCTURE OF A HYPERTHERMOPHILIC TUNGSTOPTERIN ENZYME, ALDEHYDE FERREDOXIN OXIDOREDUCTASE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1AOR is a [ | 1AOR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AOR OCA]. | ||
==Reference== | ==Reference== | ||
Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase., Chan MK, Mukund S, Kletzin A, Adams MW, Rees DC, Science. 1995 Mar 10;267(5203):1463-9. PMID:[http:// | Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase., Chan MK, Mukund S, Kletzin A, Adams MW, Rees DC, Science. 1995 Mar 10;267(5203):1463-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7878465 7878465] | ||
[[Category: Pyrococcus furiosus]] | [[Category: Pyrococcus furiosus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:00:22 2008'' | ||
Revision as of 11:00, 20 March 2008
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| , resolution 2.3Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF A HYPERTHERMOPHILIC TUNGSTOPTERIN ENZYME, ALDEHYDE FERREDOXIN OXIDOREDUCTASE
OverviewOverview
The crystal structure of the tungsten-containing aldehyde ferredoxin oxidoreductase (AOR) from Pyrococcus furiosus, a hyperthermophilic archaeon (formerly archaebacterium) that grows optimally at 100 degrees C, has been determined at 2.3 angstrom resolution by means of multiple isomorphous replacement and multiple crystal form averaging. AOR consists of two identical subunits, each containing an Fe4S4 cluster and a molybdopterin-based tungsten cofactor that is analogous to the molybdenum cofactor found in a large class of oxotransferases. Whereas the general features of the tungsten coordination in this cofactor were consistent with a previously proposed structure, each AOR subunit unexpectedly contained two molybdopterin molecules that coordinate a tungsten by a total of four sulfur ligands, and the pterin system was modified by an intramolecular cyclization that generated a three-ringed structure. In comparison to other proteins, the hyperthermophilic enzyme AOR has a relatively small solvent-exposed surface area, and a relatively large number of both ion pairs and buried atoms. These properties may contribute to the extreme thermostability of this enzyme.
About this StructureAbout this Structure
1AOR is a Single protein structure of sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA.
ReferenceReference
Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase., Chan MK, Mukund S, Kletzin A, Adams MW, Rees DC, Science. 1995 Mar 10;267(5203):1463-9. PMID:7878465
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