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PDBsum entry 4c0e
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Gene regulation
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PDB id
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4c0e
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PDB id:
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| Name: |
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Gene regulation
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Title:
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Structure of the not1 superfamily homology domain from chaetomium thermophilum
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Structure:
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Not1. Chain: a, b, c, d. Fragment: not1 superfamily homology domain, residues 1676-2193. Engineered: yes
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Source:
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Chaetomium thermophilum. Organism_taxid: 209285. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: star.
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Resolution:
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3.20Å
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R-factor:
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0.219
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R-free:
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0.259
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Authors:
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Y.Chen,A.Boland,T.Raisch,S.Jonas,E.Izaurralde,O.Weichenrieder
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Key ref:
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A.Boland
et al.
(2013).
Structure and assembly of the NOT module of the human CCR4-NOT complex.
Nat Struct Biol,
20,
1289-1297.
PubMed id:
DOI:
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Date:
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01-Aug-13
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Release date:
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09-Oct-13
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PROCHECK
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Headers
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References
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G0SAL9
(G0SAL9_CHATD) -
Uncharacterized protein from Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
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Seq:
Struc:
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2193 a.a.
508 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 2 residue positions (black
crosses)
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DOI no:
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Nat Struct Biol
20:1289-1297
(2013)
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PubMed id:
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Structure and assembly of the NOT module of the human CCR4-NOT complex.
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A.Boland,
Y.Chen,
T.Raisch,
S.Jonas,
D.Kuzuoğlu-Öztürk,
L.Wohlbold,
O.Weichenrieder,
E.Izaurralde.
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ABSTRACT
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The CCR4-NOT deadenylase complex is a master regulator of translation and mRNA
stability. Its NOT module orchestrates recruitment of the catalytic subunits to
target mRNAs. We report the crystal structure of the human NOT module formed by
the CNOT1, CNOT2 and CNOT3 C-terminal (-C) regions. CNOT1-C provides a rigid
scaffold consisting of two perpendicular stacks of HEAT-like repeats. CNOT2-C
and CNOT3-C heterodimerize through their SH3-like NOT-box domains. The
heterodimer is stabilized and tightly anchored to the surface of CNOT1 through
an unexpected intertwined arrangement of peptide regions lacking defined
secondary structure. These assembly peptides mold onto their respective binding
surfaces and form extensive interfaces. Mutagenesis of individual interfaces and
perturbation of endogenous protein ratios cause defects in complex assembly and
mRNA decay. Our studies provide a structural framework for understanding the
recruitment of the CCR4-NOT complex to mRNA targets.
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Links
