Protein Science Sheba protein
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Protein Science (2005), 14:2751-2758. Published by Cold Spring Harbor Laboratory Press. Copyright © 2005 The Protein Society
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Leulliot, N.
Right arrow Articles by Van Tilbeurgh, H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Leulliot, N.
Right arrow Articles by Van Tilbeurgh, H.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

PROTEIN STRUCTURE REPORT

Crystal structure of yeast YER010Cp, a knotable member of the RraA protein family

Nicolas Leulliot1, Sophie Quevillon-Cheruel1, Marc Graille1, Marc Schiltz3, Karine Blondeau2, Joël Janin4 and Herman Van Tilbeurgh1

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 d’Enzymologie 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.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?





HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2005 by The Protein Society.