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Crystallization and preliminary X-ray analysis of the glycogen synthase from Pyrococcus abyssi

AutorHorcajada, Cristina; Cid, Emili; Guinovart, Joan J.; Verdaguer, Núria ; Ferrer, Juan Carlos
Fecha de publicacióndic-2003
EditorBlackwell Publishing
CitaciónActa Crystallographica Section D: Biological Crystallography 59(12): 2322-2324 (2003)
ResumenGlycogen synthase catalyzes the transfer of glucosyl residues from ADP- or UDP-glucose to the non-reducing end of a growing α-1,4-glucan chain. To date, no crystallographic structure of an animal/ fungal glycogen synthase (family 3 of the glycosyl transferases) or a bacterial/plant glycogen/starch synthase (family 5) has been reported. This paper describes the recombinant expression, crystallization and preliminary X-ray analysis of the glycogen synthase from the hyperthermophilic archaeon Pyrococcus abyssi, the smallest enzyme of the members of families 3 and 5 of the glycosyl transferases. Crystals from this protein and from its selenomethionyl variant were grown in 100 mM sodium citrate pH 5.6 containing 20% PEG and 20% dioxane by the hanging-drop vapour-diffusion method at 293 K. The crystals, which grew as thin needles, diffracted to 3.5 Å resolution and belong to space group C2, with unit-cell parameters a = 202, b = 73, c = 149 Å, β = 131°. The crystallographic and biochemical data are consistent with either a dimer or a tetramer in the crystal asymmetric unit and a volume solvent content of 70 or 39%, respectively.
Versión del editorhttp://dx.doi.org/10.1107/S0907444903021279
URIhttp://hdl.handle.net/10261/110147
DOI10.1107/S0907444903021279
Identificadoresdoi: 10.1107/S0907444903021279
issn: 0907-4449
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