2rcv
From Proteopedia
Crystal structure of the Bacillus subtilis superoxide dismutase
Structural highlights
FunctionSODM_BACSU Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. Structure of Bacillus subtilis superoxide dismutase.,Liu P, Ewis HE, Huang YJ, Lu CD, Tai PC, Weber IT Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Dec 1;63(Pt, 12):1003-7. Epub 2007 Nov 21. PMID:18084079[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Categories: Bacillus subtilis | Large Structures | Ewis HE | Huang YJ | Liu P | Lu CD | Tai PC | Weber IT
