Crystallization and preliminary X-ray diffraction analysis of the catalytic subunit of ADP-glucose pyrophosphorylase from potato tuber

Carregando...
Imagem de Miniatura

Data

2000-02-01

Autores

Binderup, K.
Watanabe, L.
Polikarpov, I
Preiss, J.
Arni, R. K.

Título da Revista

ISSN da Revista

Título de Volume

Editor

Munksgaard Int Publ Ltd

Resumo

ADP-glucose pyrophosphorylase is the key regulatory enzyme in the biosynthesis of starch in plants and glycogen in bacteria. The enzyme from potato tuber is comprised of a regulatory subunit and a catalytic subunit and is present as a heterotetramer (alpha(2)beta(2)) the catalytic subunit from potato tuber (50 kDa) was crystallized in four different forms, two of which are suitable for structural studies. A tetragonal crystal form obtained in the presence of the substrate analog Cr-ATP diffracted to 2.2 Angstrom and belongs to space group P4(1) (or its enantiomorph), with unit-cell parameters a = b = 110.57, c = 190.14 Angstrom. A second crystal form obtained diffracted to 2.8 Angstrom and belongs to space group PZ, with unit-eel parameters a = 80.06, b = 138.84, c = 92.20 Angstrom, beta = 112.40 degrees. As this protein displays no significant homology to any currently known protein structure, a search for heavy-atom derivatives has been initiated.

Descrição

Palavras-chave

Como citar

Acta Crystallographica Section D-biological Crystallography. Copenhagen: Munksgaard Int Publ Ltd, v. 56, p. 192-194, 2000.