Crystallization, X-ray diffraction and oligomeric characterization of arginine decarboxylase from Yersinia pestis, a key polyamine biosynthetic enzyme

Chandra N Patel; Robert S Adcock; Korie G Sell; Marcos A Oliveira

doi:10.1107/S0907444904027180

Crystallization, X-ray diffraction and oligomeric characterization of arginine decarboxylase from Yersinia pestis, a key polyamine biosynthetic enzyme

Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 2):2396-8. doi: 10.1107/S0907444904027180. Epub 2004 Nov 26.

Authors

Chandra N Patel¹, Robert S Adcock, Korie G Sell, Marcos A Oliveira

Affiliation

¹ Department of Pharmaceutical Sciences, Markey Cancer Center and Center for Structural Biology, University of Kentucky, Kentucky, USA.

PMID: 15583399
DOI: 10.1107/S0907444904027180

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.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

Carboxy-Lyases / chemistry*
Crystallography, X-Ray / methods*
Dimerization
Light
Mercury / chemistry
Models, Chemical
Polyamines / chemistry
Scattering, Radiation
X-Ray Diffraction
Yersinia pestis / enzymology*

Substances

Polyamines
Carboxy-Lyases
arginine decarboxylase
Mercury