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PDBsum entry 4bwk
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Gene regulation
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PDB id
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4bwk
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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 neurospora crassa pan3 pseudokinase
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Structure:
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Pab-dependent poly(a)-specific ribonuclease subunit pan-3. Chain: a, b. Fragment: pseudokinase domain, coiled coil, cterminal knob, residues 234-656. Synonym: pab1p-dependent poly(a)-nuclease, pab-dependent polya- specific ribonuclease subunit pan-3. Engineered: yes
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Source:
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Neurospora crassa. Organism_taxid: 5141. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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3.30Å
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R-factor:
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0.254
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R-free:
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0.294
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Authors:
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M.Christie,A.Boland,E.Huntzinger,O.Weichenrieder,E.Izaurralde
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Key ref:
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M.Christie
et al.
(2013).
Structure of the PAN3 pseudokinase reveals the basis for interactions with the PAN2 deadenylase and the GW182 proteins.
Mol Cell,
51,
360-373.
PubMed id:
DOI:
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Date:
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04-Jul-13
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Release date:
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21-Aug-13
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PROCHECK
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Headers
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References
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Q7SDP4
(PAN3_NEUCR) -
PAN2-PAN3 deadenylation complex subunit pan3 from Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
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Seq:
Struc:
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656 a.a.
392 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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DOI no:
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Mol Cell
51:360-373
(2013)
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PubMed id:
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Structure of the PAN3 pseudokinase reveals the basis for interactions with the PAN2 deadenylase and the GW182 proteins.
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M.Christie,
A.Boland,
E.Huntzinger,
O.Weichenrieder,
E.Izaurralde.
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ABSTRACT
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The PAN2-PAN3 deadenylase complex functions in general and miRNA-mediated mRNA
degradation and is specifically recruited to miRNA targets by GW182/TNRC6
proteins. We describe the PAN3 adaptor protein crystal structure that,
unexpectedly, forms intertwined and asymmetric homodimers. Dimerization is
mediated by a coiled coil that links an N-terminal pseudokinase to a C-terminal
knob domain. The PAN3 pseudokinase binds ATP, and this function is required for
mRNA degradation in vivo. We further identified conserved surfaces required for
mRNA degradation, including the binding surface for the PAN2 deadenylase on the
knob domain. The most remarkable structural feature is the presence of a
tryptophan-binding pocket at the dimer interface, which mediates binding to
TNRC6C in human cells. Together, our data reveal the structural basis for the
interaction of PAN3 with PAN2 and the recruitment of the PAN2-PAN3 complex to
miRNA targets by TNRC6 proteins.
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Links
