1qnn
CAMBIALISTIC SUPEROXIDE DISMUTASE FROM PORPHYROMONAS GINGIVALIS
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OverviewOverview
The crystal structure of cambialistic superoxide dismutase (SOD) from, Porphyromonas gingivalis, which exhibits full activity with either Fe or, Mn at the active site, has been determined at 1.8-A resolution by, molecular replacement and refined to a crystallographic R factor of 17.9%, (Rfree 22.3%). The crystals belong to the space group P212121 (a = 75.5 A, b = 102.7 A, c = 99.6 A) with four identical subunits in the asymmetric, unit. Each pair of subunits forms a compact dimer, but not a tetramer, with 222 point symmetry. Each subunit has 191 amino-acid residues most of, which are visible in electron density maps, and consists of seven alpha, helices and one three-stranded antiparallel beta sheet. The metal ion, a 3, : 1 mixture of Fe and Mn, is coordinated with five ligands (His27, His74, His161, Asp157, and water) arranged at the vertices of a trigonal, bipyramid. Although the overall structural features, including the metal, coordination geometry, are similar to those found in other single-metal, containing SODs, P. gingivalis SOD more closely resembles the dimeric, Fe-SODs from Escherichia coli rather than another cambialistic SOD from, Propionibacterium shermanii, which itself is rather similar to other, tetrameric SODs.
About this StructureAbout this Structure
1QNN is a Single protein structure of sequence from Porphyromonas gingivalis with FE as ligand. Active as Superoxide dismutase, with EC number 1.15.1.1 Known structural/functional Sites: , , and . Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of cambialistic superoxide dismutase from porphyromonas gingivalis., Sugio S, Hiraoka BY, Yamakura F, Eur J Biochem. 2000 Jun;267(12):3487-95. PMID:10848964
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