Journal
EUROPEAN JOURNAL OF BIOCHEMISTRY
Volume 267, Issue 12, Pages 3487-3495Publisher
BLACKWELL SCIENCE LTD
DOI: 10.1046/j.1432-1327.2000.01373.x
Keywords
crystal structure; cambialistic superoxide dismutase; iron superoxide dismutase; manganese superoxide dismutase
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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-Angstrom resolution by molecular replacement and refined to a crystallographic R factor of 17.9% (R-free 22.3%). The crystals belong to the space group P2(1)2(1)2(1) (a = 75.5 Angstrom, b = 102.7 Angstrom, c = 99.6 Angstrom) 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 a 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.
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