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 activ...

Full description

Saved in:
Bibliographic Details
Published in:Protein science 2005-10, Vol.14 (10), p.2751-2758
Main Authors: Leulliot, Nicolas, Quevillon‐Cheruel, Sophie, Graille, Marc, Schiltz, Marc, Blondeau, Karine, Janin, Joël, Van Tilbeurgh, Herman
Format: Article
Language:English
Subjects:
crystal structure
Crystallography, X-Ray
Cystine Knot Motifs
Escherichia coli
Escherichia coli Proteins - chemistry
Escherichia coli Proteins - genetics
Multigene Family - genetics
ORF, open reading frame
Protein Structure Report
Protein Structure, Tertiary
pseudo‐knot
RMSD, root‐mean‐square deviation
Saccharomyces cerevisiae - chemistry
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae Proteins - chemistry
Saccharomyces cerevisiae Proteins - genetics
Saccharomyces cerevisiae Proteins - metabolism
SDS PAGE, sodium dodecyl sulphate polyacrylamide gel electrophoresis
SG, structural genomics
structural genomics
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:0961-8368
1469-896X
DOI:10.1110/ps.051684005