Crystallization, X-ray diffraction and oligomeric characterization of arginine decarboxylase from Yersinia pestis, a key polyamine biosynthetic enzyme.
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.
Patel
Chandra N
CN
Department of Pharmaceutical Sciences, Markey Cancer Center and Center for Structural Biology, University of Kentucky, Kentucky, USA.
Adcock
Robert S
RS
Sell
Korie G
KG
Oliveira
Marcos A
MA
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*
D011073:Polyamines; D002262:Carboxy-Lyases; C019722:arginine decarboxylase; D008628:Mercury