2rcv
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(New page: 200px<br /><applet load="2rcv" size="350" color="white" frame="true" align="right" spinBox="true" caption="2rcv, resolution 1.60Å" /> '''Crystal structure of...)
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Revision as of 05:59, 27 February 2008
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Crystal structure of the Bacillus subtilis superoxide dismutase
Overview
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.
About this Structure
2RCV is a Single protein structure of sequence from Bacillus subtilis with 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.
Reference
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
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