Crystal structure of yeast YER010Cp, a knotable member of the RraA protein family.
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.
Leulliot
Nicolas
N
Institut de Biochimie et de Biophysique Moléculaire et Cellulaire (CNRS-UMR 8619), Université Paris-Sud, Bâtiment 430, 91405 Orsay, France. Nicolas.leulliot@ibbmc.u-psud.fr
Quevillon-Cheruel
Sophie
S
Graille
Marc
M
Schiltz
Marc
M
Blondeau
Karine
K
Janin
Joël
J
Van Tilbeurgh
Herman
H
D018360:Crystallography, X-Ray; D047168:Cystine Knot Motifs; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000235:genetics; D005810:Multigene Family / Q000235:genetics; D017434:Protein Structure, Tertiary; D012441:Saccharomyces cerevisiae / Q000737:chemistry* / Q000235:genetics; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D029968:Escherichia coli Proteins; C477942:RraA protein, E coli; D029701:Saccharomyces cerevisiae Proteins; C506520:YER010C protein, S cerevisiae