Preliminary crystallographic analysis of ADP-glucose pyrophosphorylase from Agrobacterium tumefaciens

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2005-03, Vol.61 (3), p.266-268
• Main Authors: Cupp-Vickery, Jill R., Igarashi, Robert Y., Meyer, Christopher R.
• Format: Article
• Language: English
• Subjects: ADP-glucose pyrophosphorylase; Agrobacterium tumefaciens - enzymology; Bacterial Proteins - chemistry; Bacterial Proteins - isolation & purification; CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALLIZATION; Crystallization Communications; CRYSTALS; GLUCOSE; Glucose-1-Phosphate Adenylyltransferase - chemistry; Glucose-1-Phosphate Adenylyltransferase - isolation & purification; Protein Conformation; X-RAY DIFFRACTION
• ISSN: 1744-3091; 1744-3091
• DOI: 10.1107/S1744309105002265

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 Å 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 Å. 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 Å and space group I222.