2dxl
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Glycerophosphodiesterase from Enterobacter aerogenes
OverviewOverview
The structure of the glycerophosphodiesterase (GDPD) from Enterobacter, aerogenes, GpdQ, has been solved by SAD phasing from the active site metal, ions. Structural analysis indicates that GpdQ belongs to the alpha/beta, sandwich metallo-phosphoesterase family, rather than the (alpha/beta)(8), barrel GDPD family, suggesting that GpdQ is a structurally novel GDPD., Hexameric GpdQ is generated by interactions between three dimers. The, dimers are formed through domain swapping, stabilised by an inter-chain, disulfide bond, and beta-sheet extension. The active site contains a, binuclear metal centre, with a fully occupied alpha-metal ion site, and, partially occupied beta-metal ion site, as revealed by anomalous, scattering analysis. Using a combination of TLS refinement and normal mode, analysis, the dynamic movement of GpdQ was investigated. This analysis, suggests that the hexameric quaternary structure stabilises the base of, the dimer, which promotes "breathing" of the active site cleft. Comparison, with other metallo-phosphodiesterases shows that although the central, catalytic, domain is highly conserved, many of these enzymes possess, structurally unrelated secondary domains located at the entrance of the, active site. We suggest that this could be a common structural feature of, metallo-phosphodiesterases that constrains substrate specificity, preventing non-specific phosphodiester hydrolysis.
About this StructureAbout this Structure
2DXL is a Single protein structure of sequence from Enterobacter aerogenes with as ligand. Active as Glycerophosphodiester phosphodiesterase, with EC number 3.1.4.46 Full crystallographic information is available from OCA.
ReferenceReference
The structure and function of a novel glycerophosphodiesterase from Enterobacter aerogenes., Jackson CJ, Carr PD, Liu JW, Watt SJ, Beck JL, Ollis DL, J Mol Biol. 2007 Apr 6;367(4):1047-62. Epub 2007 Jan 20. PMID:17306828
Page seeded by OCA on Wed Jan 23 15:10:39 2008