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PDBsum entry 2vc8
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Protein binding
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PDB id
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2vc8
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Contents |
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* Residue conservation analysis
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Mol Cell Biol
27:8600-8611
(2007)
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PubMed id:
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A divergent Sm fold in EDC3 proteins mediates DCP1 binding and P-body targeting.
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F.Tritschler,
A.Eulalio,
V.Truffault,
M.D.Hartmann,
S.Helms,
S.Schmidt,
M.Coles,
E.Izaurralde,
O.Weichenrieder.
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ABSTRACT
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Members of the (L)Sm (Sm and Sm-like) protein family are found across all
kingdoms of life and play crucial roles in RNA metabolism. The P-body component
EDC3 (enhancer of decapping 3) is a divergent member of this family that
functions in mRNA decapping. EDC3 is composed of a N-terminal LSm domain, a
central FDF domain, and a C-terminal YjeF-N domain. We show that this modular
architecture enables EDC3 to interact with multiple components of the decapping
machinery, including DCP1, DCP2, and Me31B. The LSm domain mediates DCP1 binding
and P-body localization. We determined the three-dimensional structures of the
LSm domains of Drosophila melanogaster and human EDC3 and show that the domain
adopts a divergent Sm fold that lacks the characteristic N-terminal alpha-helix
and has a disrupted beta4-strand. This domain remains monomeric in solution and
lacks several features that canonical (L)Sm domains require for binding RNA. The
structures also revealed a conserved patch of surface residues that are required
for the interaction with DCP1 but not for P-body localization. The conservation
of surface and of critical structural residues indicates that LSm domains in
EDC3 proteins adopt a similar fold that has separable novel functions that are
absent in canonical (L)Sm proteins.
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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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G.Haas,
J.E.Braun,
C.Igreja,
F.Tritschler,
T.Nishihara,
and
E.Izaurralde
(2010).
HPat provides a link between deadenylation and decapping in metazoa.
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J Cell Biol,
189,
289-302.
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M.Larance,
A.F.Rowland,
K.L.Hoehn,
D.T.Humphreys,
T.Preiss,
M.Guilhaus,
and
D.E.James
(2010).
Global phosphoproteomics identifies a major role for AKT and 14-3-3 in regulating EDC3.
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Mol Cell Proteomics,
9,
682-694.
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S.Dong,
A.Jacobson,
and
F.He
(2010).
Degradation of YRA1 Pre-mRNA in the cytoplasm requires translational repression, multiple modular intronic elements, Edc3p, and Mex67p.
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PLoS Biol,
8,
e1000360.
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F.Tritschler,
J.E.Braun,
A.Eulalio,
V.Truffault,
E.Izaurralde,
and
O.Weichenrieder
(2009).
Structural basis for the mutually exclusive anchoring of P body components EDC3 and Tral to the DEAD box protein DDX6/Me31B.
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Mol Cell,
33,
661-668.
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PDB codes:
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F.Tritschler,
J.E.Braun,
C.Motz,
C.Igreja,
G.Haas,
V.Truffault,
E.Izaurralde,
and
O.Weichenrieder
(2009).
DCP1 forms asymmetric trimers to assemble into active mRNA decapping complexes in metazoa.
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Proc Natl Acad Sci U S A,
106,
21591-21596.
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PDB codes:
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D.G.Scofield,
and
M.Lynch
(2008).
Evolutionary diversification of the Sm family of RNA-associated proteins.
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Mol Biol Evol,
25,
2255-2267.
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F.Tritschler,
A.Eulalio,
S.Helms,
S.Schmidt,
M.Coles,
O.Weichenrieder,
E.Izaurralde,
and
V.Truffault
(2008).
Similar modes of interaction enable Trailer Hitch and EDC3 to associate with DCP1 and Me31B in distinct protein complexes.
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Mol Cell Biol,
28,
6695-6708.
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PDB codes:
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M.Jinek,
A.Eulalio,
A.Lingel,
S.Helms,
E.Conti,
and
E.Izaurralde
(2008).
The C-terminal region of Ge-1 presents conserved structural features required for P-body localization.
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RNA,
14,
1991-1998.
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PDB code:
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S.H.Ling,
C.J.Decker,
M.A.Walsh,
M.She,
R.Parker,
and
H.Song
(2008).
Crystal structure of human Edc3 and its functional implications.
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Mol Cell Biol,
28,
5965-5976.
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PDB codes:
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T.M.Franks,
and
J.Lykke-Andersen
(2008).
The control of mRNA decapping and P-body formation.
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Mol Cell,
32,
605-615.
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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
codes are
shown on the right.
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Links
