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PDBsum entry 5elk
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RNA binding protein/RNA
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PDB id
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5elk
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PDB id:
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| Name: |
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RNA binding protein/RNA
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Title:
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Crystal structure of mouse unkempt zinc fingers 4-6 (znf4-6), bound to RNA
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Structure:
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Ring finger protein unkempt homolog. Chain: a. Fragment: unp residues 204-335. Synonym: zinc finger ccch domain-containing protein 5. Engineered: yes. RNA. Chain: r. Engineered: yes
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Source:
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Mus musculus. Mouse. Organism_taxid: 10090. Gene: unk, kiaa1753, zc3h5, zc3hdc5. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Organism_taxid: 10090
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Resolution:
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2.30Å
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R-factor:
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0.182
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R-free:
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0.224
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Authors:
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M.Teplova,J.Murn,K.Zarnack,Y.Shi,D.J.Patel
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Key ref:
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J.Murn
et al.
(2016).
Recognition of distinct RNA motifs by the clustered CCCH zinc fingers of neuronal protein Unkempt.
Nat Struct Biol,
23,
16-23.
PubMed id:
DOI:
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Date:
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04-Nov-15
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Release date:
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09-Dec-15
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PROCHECK
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Headers
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References
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Q8BL48
(UNK_MOUSE) -
RING finger protein unkempt homolog from Mus musculus
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Seq: Struc:
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810 a.a.
121 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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DOI no:
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Nat Struct Biol
23:16-23
(2016)
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PubMed id:
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Recognition of distinct RNA motifs by the clustered CCCH zinc fingers of neuronal protein Unkempt.
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J.Murn,
M.Teplova,
K.Zarnack,
Y.Shi,
D.J.Patel.
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ABSTRACT
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Unkempt is an evolutionarily conserved RNA-binding protein that regulates
translation of its target genes and is required for the establishment of the
early bipolar neuronal morphology. Here we determined the X-ray crystal
structure of mouse Unkempt and show that its six CCCH zinc fingers (ZnFs) form
two compact clusters, ZnF1-3 and ZnF4-6, that recognize distinct trinucleotide
RNA substrates. Both ZnF clusters adopt a similar overall topology and use
distinct recognition principles to target specific RNA sequences.
Structure-guided point mutations reduce the RNA binding affinity of Unkempt both
in vitro and in vivo, ablate Unkempt's translational control and impair the
ability of Unkempt to induce a bipolar cellular morphology. Our study unravels a
new mode of RNA sequence recognition by clusters of CCCH ZnFs that is critical
for post-transcriptional control of neuronal morphology.
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');
}
}
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