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1 Institut de Biochimie et de Biophysique Moléculaire et Cellulaire (CNRS-UMR 8619) and 2 Institut de Génétique et Microbiologie (CNRS-UMR 8621), Université Paris-Sud, 91405 Orsay, France
3 Ecole Polytechnique Fédérale de Lausanne (EPFL), Laboratoire de Cristallographie, CH-1015 Lausanne, Switzerland
4 Laboratoire dEnzymologie et Biochimie Structurales (CNRS-UPR 9063), 91198 Gif sur Yvette, France
(RECEIVED July 7, 2005; FINAL REVISION July 7, 2005; ACCEPTED July 15, 2005)
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.
Keywords: structural genomics; crystal structure; pseudo-knot
Abbreviations: SDS PAGE, sodium dodecyl sulphate polyacrylamide gel electrophoresis ORF, open reading frame SG, structural genomics RMSD, root-mean-square deviation.
Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.051684005.
Reprint requests to: Nicolas Leulliot, Institut de Biochimie et de Biophysique Moléculaire et Cellulaire (CNRS-UMR 8619), Université Paris-Sud, Bâtiment 430, 91405 Orsay, France; e-mail: Nicolas.leulliot{at}ibbmc.u-psud.fr; fax: +33-1-69853715.
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