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PDBsum entry 6tqb
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RNA binding protein
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PDB id
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6tqb
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PDB id:
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| Name: |
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RNA binding protein
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Title:
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X-ray structure of roquin roq domain in complex with a ucp3 cde1 sl RNA motif
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Structure:
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Roquin-1. Chain: a. Synonym: roquin,protein sanroque,ring finger and c3h zinc finger protein 1,ring finger and ccch-type zinc finger domain-containing protein 1. Engineered: yes. RNA (5'- r(p Gp Gp Ap Ap Ap Up Up Ap Up Ap Up Up Ap Ap Up Up Up Cp C)-3'). Chain: b.
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Source:
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Mus musculus. House mouse. Organism_taxid: 10090. Gene: rc3h1, gm551, kiaa2025. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Organism_taxid: 10090
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Resolution:
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1.60Å
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R-factor:
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0.158
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R-free:
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0.197
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Authors:
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O.Binas,J.-N.Tants,S.A.Peter,R.Janowski,E.Davydova,J.Braun, D.Niessing,H.Schwalbe,J.E.Weigand,A.Schlundt
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Key ref:
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O.Binas
et al.
(2020).
Structural basis for the recognition of transiently structured AU-rich elements by Roquin.
Nucleic Acids Res,
48,
7385-7403.
PubMed id:
DOI:
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Date:
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16-Dec-19
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Release date:
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27-May-20
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PROCHECK
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Headers
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References
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Q4VGL6
(RC3H1_MOUSE) -
Roquin-1 from Mus musculus
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Seq:
Struc:
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1130 a.a.
154 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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G-G-A-A-A-U-U-A-U-A-U-U-A-A-U-U-U-C-C
19 bases
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Enzyme class:
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E.C.2.3.2.27
- RING-type E3 ubiquitin transferase.
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Reaction:
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S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6- ubiquitinyl-[acceptor protein]-L-lysine
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DOI no:
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Nucleic Acids Res
48:7385-7403
(2020)
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PubMed id:
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Structural basis for the recognition of transiently structured AU-rich elements by Roquin.
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O.Binas,
J.N.Tants,
S.A.Peter,
R.Janowski,
E.Davydova,
J.Braun,
D.Niessing,
H.Schwalbe,
J.E.Weigand,
A.Schlundt.
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ABSTRACT
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Adenylate/uridylate-rich elements (AREs) are the most common cis-regulatory
elements in the 3'-untranslated region (UTR) of mRNAs, where they fine-tune
turnover by mediating mRNA decay. They increase plasticity and efficacy of mRNA
regulation and are recognized by several ARE-specific RNA-binding proteins
(RBPs). Typically, AREs are short linear motifs with a high content of
complementary A and U nucleotides and often occur in multiple copies. Although
thermodynamically rather unstable, the high AU-content might enable transient
secondary structure formation and modify mRNA regulation by RBPs. We have
recently suggested that the immunoregulatory RBP Roquin recognizes folded AREs
as constitutive decay elements (CDEs), resulting in shape-specific ARE-mediated
mRNA degradation. However, the structural evidence for a CDE-like recognition of
AREs by Roquin is still lacking. We here present structures of CDE-like folded
AREs, both in their free and protein-bound form. Moreover, the AREs in the UCP3
3'-UTR are additionally bound by the canonical ARE-binding protein AUF1 in their
linear form, adopting an alternative binding-interface compared to the
recognition of their CDE structure by Roquin. Strikingly, our findings thus
suggest that AREs can be recognized in multiple ways, allowing control over mRNA
regulation by adapting distinct conformational states, thus providing
differential accessibility to regulatory RBPs.
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Links
