Jackson, Colin J. and Hadler, Kieran S. and Carr, Paul D. and Oakley, Aaron J. and Yip, Sylvia and Schenk, Gerhard and Ollis, David L.
Malonate-bound structure of the
glycerophosphodiesterase from Enterobacter
aerogenes (GpdQ) and characterization of the
native Fe2+ metal-ion preference.
Acta Crystallographica Section F, 64 (8).
The structure of a malonate-bound form of the glycerophosphodiesterase from
Enterobacter aerogenes, GpdQ, has been refined at a resolution of 2.2 A ° to a
final R factor of 17.1%. The structure was originally solved to 2.9 A ° resolution
using SAD phases from Zn2+ metal ions introduced into the active site of the
apoenzyme [Jackson et al. (2007), J. Mol. Biol. 367, 1047–1062]. However, the
2.9 A ° resolution was insufficient to discern significant details of the architecture
of the binuclear metal centre that constitutes the active site. Furthermore,
kinetic analysis revealed that the enzyme lost a significant amount of activity in
the presence of Zn2+, suggesting that it is unlikely to be a catalytically relevant
metal ion. In this communication, a higher resolution structure of GpdQ is
presented in which malonate is visibly coordinated in the active site and analysis
of the native metal-ion preference is presented using atomic absorption
spectroscopy and anomalous scattering. Catalytic implications of the structure
and its Fe2+ metal-ion preference are discussed.
||The definitive version of this article is published in Acta Crystallographica Section F, 2008, v.64 n.8,
||Malonate-bound; glycerophosphodiesterase; Enterobacter
aerogenes (GpdQ); Fe2+ metal-ion preference;
||Faculty of Science and Engineering > Chemistry
||30 May 2012 15:49
|Journal or Publication Title:
||Acta Crystallographica Section F
||International Union of Crystallography
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