Crystal structure of yeast YER010Cp, aknotable member of the RraA protein family

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Leulliot, Nicolas | Quevillon-Cheruel, Sophie | Graille, Marc | Schiltz, Marc | Blondeau, Karine | Janin, Joël | van Tilbeurgh, Herman

Edité par CCSD ; Wiley -

International audience. We present here the structure of Yer010c protein of unknown function, solved by Multiple Anomalous Diffraction and revealing a common fold and oligomerization state with proteins of the regulator of ribonuclease activity A (RraA) family. In Escherichia coli, RraA has been shown to regulate the activity of ribonuclease E by direct interaction. The absence of ribonuclease E in yeast suggests a different function for this family member in this organism. Yer010cp has a few supplementary secondary structure elements and a deep pseudo-knot at the heart of the protein core. A tunnel at the interface between two monomers, lined with conserved charged residues, has unassigned residual electron density and may constitute an active site for a yet unknown activity.

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