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RNA-binding protein
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PDB id
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2uy1
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* Residue conservation analysis
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Gene Ontology (GO) functional annotation
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Cellular component
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intracellular
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2 terms
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Biological process
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RNA processing
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2 terms
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DOI no:
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Nucleic Acids Res
35:4515-4522
(2007)
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PubMed id:
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The structure of the CstF-77 homodimer provides insights into CstF assembly.
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P.Legrand,
N.Pinaud,
L.Minvielle-Sébastia,
S.Fribourg.
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ABSTRACT
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The cleavage stimulation factor (CstF) is essential for the first step of
poly(A) tail formation at the 3' ends of mRNAs. This heterotrimeric complex is
built around the 77-kDa protein bridging both CstF-64 and CstF-50 subunits. We
have solved the crystal structure of the 77-kDa protein from Encephalitozoon
cuniculi at a resolution of 2 A. The structure folds around 11 Half-a-TPR
repeats defining two domains. The crystal structure reveals a tight homodimer
exposing phylogenetically conserved areas for interaction with protein partners.
Mapping experiments identify the C-terminal region of Rna14p, the yeast
counterpart of CstF-77, as the docking domain for Rna15p, the yeast CstF-64
homologue.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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C.D.Mackereth
(2011).
Chemical shift assignments of a minimal Rna14p/Rna15p heterodimer from the yeast cleavage factor IA complex.
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Biomol NMR Assign, 5,
93-95.
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M.Moreno-Morcillo,
L.Minvielle-Sébastia,
S.Fribourg,
and
C.D.Mackereth
(2011).
Locked tether formation by cooperative folding of Rna14p monkeytail and Rna15p hinge domains in the yeast CF IA complex.
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Structure, 19,
534-545.
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PDB code:
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C.Pancevac,
D.C.Goldstone,
A.Ramos,
and
I.A.Taylor
(2010).
Structure of the Rna15 RRM-RNA complex reveals the molecular basis of GU specificity in transcriptional 3'-end processing factors.
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Nucleic Acids Res, 38,
3119-3132.
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PDB codes:
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J.A.Hockert,
H.J.Yeh,
and
C.C.MacDonald
(2010).
The hinge domain of the cleavage stimulation factor protein CstF-64 is essential for CstF-77 interaction, nuclear localization, and polyadenylation.
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J Biol Chem, 285,
695-704.
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E.A.Champion,
L.Kundrat,
L.Regan,
and
S.J.Baserga
(2009).
A structural model for the HAT domain of Utp6 incorporating bioinformatics and genetics.
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Protein Eng Des Sel, 22,
431-439.
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G.A.Palidwor,
S.Shcherbinin,
M.R.Huska,
T.Rasko,
U.Stelzl,
A.Arumughan,
R.Foulle,
P.Porras,
L.Sanchez-Pulido,
E.E.Wanker,
and
M.A.Andrade-Navarro
(2009).
Detection of alpha-rod protein repeats using a neural network and application to huntingtin.
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PLoS Comput Biol, 5,
e1000304.
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Y.Shi,
D.C.Di Giammartino,
D.Taylor,
A.Sarkeshik,
W.J.Rice,
J.R.Yates,
J.Frank,
and
J.L.Manley
(2009).
Molecular architecture of the human pre-mRNA 3' processing complex.
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Mol Cell, 33,
365-376.
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E.A.Champion,
B.H.Lane,
M.E.Jackrel,
L.Regan,
and
S.J.Baserga
(2008).
A direct interaction between the Utp6 half-a-tetratricopeptide repeat domain and a specific peptide in Utp21 is essential for efficient pre-rRNA processing.
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Mol Cell Biol, 28,
6547-6556.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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