2RCV
Crystal structure of the Bacillus subtilis superoxide dismutase
Summary for 2RCV
Entry DOI | 10.2210/pdb2rcv/pdb |
Descriptor | Superoxide dismutase [Mn], MANGANESE (II) ION (3 entities in total) |
Functional Keywords | bacillus subtilis, superoxide dismutase, manganese, metal-binding, oxidoreductase, phosphorylation, stress response |
Biological source | Bacillus subtilis |
Cellular location | Cytoplasm : P54375 |
Total number of polymer chains | 8 |
Total formula weight | 181239.41 |
Authors | Liu, P.,Ewis, H.E.,Huang, Y.J.,Lu, C.D.,Tai, P.C.,Weber, I.T. (deposition date: 2007-09-20, release date: 2008-02-26, Last modification date: 2023-08-30) |
Primary citation | Liu, P.,Ewis, H.E.,Huang, Y.J.,Lu, C.D.,Tai, P.C.,Weber, I.T. Structure of Bacillus subtilis superoxide dismutase. Acta Crystallogr.,Sect.F, 63:1003-1007, 2007 Cited by PubMed Abstract: The sodA gene of Bacillus subtilis was expressed in Escherichia coli, purified and crystallized. The crystal structure of MnSOD was solved by molecular replacement with four dimers per asymmetric unit and refined to an R factor of 21.1% at 1.8 A resolution. The dimer structure is very similar to that of the related enzyme from B. anthracis. Larger structural differences were observed with the human MnSOD, which has one less helix in the helical domain and a longer loop between two beta-strands and also showed differences in three amino acids at the intersubunit interface in the dimer compared with the two bacterial MnSODs. These structural differences can be exploited in the design of drugs that selectively target the Bacillus enzymes. PubMed: 18084079DOI: 10.1107/S1744309107054127 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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