Preliminary crystallographic analysis of ADP-glucose pyrophosphorylase from Agrobacterium tumefaciens.
ADP-glucose pyrophosphorylase catalyzes the conversion of glucose-1-phosphate and ATP to ADP-glucose and pyrophosphate, a key regulated step in both bacterial glycogen and plant starch biosynthesis. Crystals of ADP-glucose pyrophosphorylase from Agrobacterium tumefaciens (420 amino acids, 47 kDa) have been obtained by the sitting-drop vapor-diffusion method using lithium sulfate as a precipitant. A complete native X-ray diffraction data set was collected to a resolution of 2.0 A from a single crystal at 100 K. The crystals belong to space group I222, with unit-cell parameters a = 92.03, b = 141.251, c = 423.64 A. To solve the phase problem, a complete anomalous data set was collected from a selenomethionyl derivative. These crystals display one-fifth of the unit-cell volume of the wild-type crystals, with unit-cell parameters a = 85.38, b = 93.79, c = 140.29 A and space group I222.
Cupp-Vickery
Jill R
JR
Department of Physiology and Biophysics, University of California, Irvine, CA 92697, USA. jvickery@uci.edu
Igarashi
Robert Y
RY
Meyer
Christopher R
CR
D016960:Agrobacterium tumefaciens / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification; D051599:Glucose-1-Phosphate Adenylyltransferase / Q000737:chemistry* / Q000302:isolation & purification; D011487:Protein Conformation; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D051599:Glucose-1-Phosphate Adenylyltransferase