title: Crystallization, X-ray diffraction and oligomeric characterization of arginine decarboxylase from Yersinia pestis, a key polyamine biosynthetic enzyme.
abstract: Arginine decarboxylase (ADC) is a 70 kDa pyridoxal-5'-phosphate (PLP) dependent enzyme that controls an alternative step in the biosynthesis of polyamines in some bacteria and plants. Crystals of ADC were flash-cooled and diffracted to 3.0 A resolution using a synchrotron-radiation source. Crystals of ADC are monoclinic, with four monomers in the asymmetric unit. Light-scattering data reveals that the enzyme forms dimers in solution. The rotation function suggests the presence of two dimers in the asymmetric unit. Heavy-atom searches have identified PCMBS as forming a mercury derivative.
authors.affiliation: Department of Pharmaceutical Sciences, Markey Cancer Center and Center for Structural Biology, University of Kentucky, Kentucky, USA.
authors.forename: Chandra N
authors.initials: CN
authors.lastname: Patel
authors.forename: Robert S
authors.initials: RS
authors.lastname: Adcock
authors.forename: Korie G
authors.initials: KG
authors.lastname: Sell
authors.forename: Marcos A
authors.initials: MA
authors.lastname: Oliveira
mesh_terms: D002262:Carboxy-Lyases / Q000737:chemistry*; D018360:Crystallography, X-Ray / Q000379:methods*; D019281:Dimerization; D008027:Light; D008628:Mercury / Q000737:chemistry; D008956:Models, Chemical; D011073:Polyamines / Q000737:chemistry; D012542:Scattering, Radiation; D014961:X-Ray Diffraction; D015010:Yersinia pestis / Q000201:enzymology*
chemical_list: D011073:Polyamines; D002262:Carboxy-Lyases; C019722:arginine decarboxylase; D008628:Mercury