PMID:10957638

Citation	Cronk, JD, O'Neill, JW, Cronk, MR, Endrizzi, JA and Zhang, KY (2000) Cloning, crystallization and preliminary characterization of a beta-carbonic anhydrase from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 56:1176-9
Abstract	Carbonic anhydrases are zinc metalloenzymes that fall into three distinct evolutionary and structural classes, alpha, beta and gamma. Although alpha-class enzymes, particularly mammalian carbonic anhydrase II, have been the subject of extensive structural studies, for the beta class, consisting of a wide variety of prokaryotic and plant chloroplast carbonic anhydrases, the structural data is quite limited. A member of the beta class from E. coli (CynT2) has been crystallized in native and selenomethionine-labelled forms and multiwavelength anomalous dispersion techniques have been applied in order to determine the positions of anomalous scatterers. The resulting phase information is sufficient to produce an interpretable electron-density map. A crystal structure for CynT2 would contribute significantly to the emerging structural knowledge of a biologically important class of enzymes that perform critical functions in carbon fixation and prokaryotic metabolism.
Links	PubMed
Keywords	Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Carbonic Anhydrases/chemistry; Carbonic Anhydrases/genetics; Cations; Cloning, Molecular; Crystallization; Crystallography, X-Ray; Escherichia coli/enzymology; Escherichia coli/genetics; Isoenzymes/chemistry; Isoenzymes/genetics; Selenium/chemistry; Selenomethionine/chemistry; Zinc/chemistry
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