Crystal Structure of Yeast Allantoicase Reveals a Repeated Jelly Roll Motif

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Leulliot, Nicolas | Quevillon-Cheruel, Sophie | Sorel, Isabelle | Graille, Marc | Meyer, Philippe | Liger, Dominique | Blondeau, Karine | Janin, Joël | van Tilbeurgh, Herman

Edité par CCSD ; American Society for Biochemistry and Molecular Biology -

International audience. Allantoicase (EC 3.5.3.4) catalyzes the conversion of allantoate into ureidoglycolate and urea, one of the final steps in the degradation of purines to urea. The mechanism of most enzymes involved in this pathway, which has been known for a long time, is unknown. In this paper we describe the three-dimensional crystal structure of the yeast allantoicase determined at a resolution of 2.6 Å by single anomalous diffraction. This constitutes the first structure for an enzyme of this pathway. The structure reveals a repeated jelly roll β-sheet motif, also present in proteins of unrelated biochemical function. Allantoicase has a hexameric arrangement in the crystal (dimer of trimers). Analysis of the protein sequence against the structural data reveals the presence of two totally conserved surface patches, one on each jelly roll motif. The hexameric packing concentrates these patches into conserved pockets that probably constitute the active site.

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