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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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References listed in PDB file
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Key reference
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Title
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A divergent sm fold in edc3 proteins mediates dcp1 binding and p-Body targeting.
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Authors
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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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Ref.
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Mol Cell Biol, 2007,
27,
8600-8611.
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PubMed id
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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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