1wb8
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IRON SUPEROXIDE DISMUTASE (FE-SOD) FROM THE HYPERTHERMOPHILE SULFOLOBUS SOLFATARICUS. 2.3 A RESOLUTION STRUCTURE OF RECOMBINANT PROTEIN WITH A COVALENTLY MODIFIED TYROSIN IN THE ACTIVE SITE.
OverviewOverview
The crystal structure of superoxide dismutase (SOD) from the hyper, thermophile Sulfolobus solfataricus has been determined at 2.3 A, resolution by molecular replacement and refined to a crystallographic, R-factor of 16.8 % (Rfree 19.8 %). The crystals belong to the space group, C2 (a=76.3 A, b=124.3 A, c=60.3 A, beta=128.8 degrees) with two identical, monomers in the asymmetric unit. The monomer has a molecular weight of 24, kDa and consists of 210 amino acid residues of which 205 are visible in, the electron density map. The overall fold of the monomer of S., solfataricus SOD is similar to that of the other known Fe or Mn-SODs. S., solfataricus SOD forms a very compact tetramer of a type similar to that, of SOD from the hyperthermophile Aquifex pyrophilus. Both structures show, an ... [(full description)]
About this StructureAbout this Structure
1WB8 is a [Single protein] structure of sequence from [Sulfolobus solfataricus] with FE and PMS as [ligands]. This structure superseeds the now removed PDB entry 1SSS. Active as [Superoxide dismutase], with EC number [1.15.1.1]. Structure known Active Site: FEA. Full crystallographic information is available from [OCA].
ReferenceReference
Iron superoxide dismutase from the archaeon Sulfolobus solfataricus: analysis of structure and thermostability., Ursby T, Adinolfi BS, Al-Karadaghi S, De Vendittis E, Bocchini V, J Mol Biol. 1999 Feb 12;286(1):189-205. PMID:9931259
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