Crystallographic studies of the structured core domain of Knr4 fromSaccharomyces cerevisiae

Sylviane Julien (1) , Patrick Tondl (1) , Fabien Durand (2) , Adilia Dagkessamanskaia (2) , Herman van Tilbeurgh (3) , Jean Marie François (2) , Lionel Mourey (1) , Didier Zerbib (1, 2) , Hélène Martin-Yken (2) , Laurent Maveyraud (1)

1 IPBS - Institut de pharmacologie et de biologie structurale
2 LISBP - Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés
3 I2BC - Institut de Biologie Intégrative de la Cellule

The potentially structured core domain of the intrinsically disordered protein Knr4 from Saccharomyces cerevisiae, comprising residues 80-340, was expressed in Escherichia coli and crystallized using the hanging-drop vapour-diffusion method. Selenomethionine-containing (SeMet) protein was also purified and crystallized. Crystals of both proteins belonged to space group P6 5 22, with unit-cell parameters a = b = 112.44, c = 265.21 Å for the native protein and a = b = 112.49, c = 262.21 Å for the SeMet protein, and diffracted to 3.50 and 3.60 Å resolution, respectively. There are two molecules in the asymmetric unit related by a twofold axis. The anomalous signal of selenium was recorded and yielded an electron-density map of sufficient quality to allow the identification of secondary-structure elements.

Mots clés: intrinsically disordered proteins; hub proteins; Saccharomyces cerevisiae; cell-wall biogenesis regulation

Domaines: Sciences du Vivant [q-bio]

Sylviane Julien, Patrick Tondl, Fabien Durand, Adilia Dagkessamanskaia, Herman van Tilbeurgh, et al.. Crystallographic studies of the structured core domain of Knr4 fromSaccharomyces cerevisiae. Acta crystallographica Section F : Structural biology communications [2014-..], 2015, 71 (9), pp.1120 - 1124. ⟨10.1107/s2053230x15012522⟩. ⟨hal-03002962⟩