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PDBsum entry 2ynn
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Protein transport
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PDB id
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2ynn
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PDB id:
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| Name: |
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Protein transport
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Title:
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Yeast betaprime cop 1-304 with ktktn motif
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Structure:
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Coatomer subunit beta'. Chain: a. Fragment: wd40-repeat domain, residues 1-304. Synonym: beta'-coat protein, beta'-cop. Engineered: yes. Other_details: in complex with kxkxx motif. Ktktn motif. Chain: p. Engineered: yes
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Source:
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Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: plyss. Synthetic: yes. Synthetic construct. Organism_taxid: 32630
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Resolution:
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1.78Å
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R-factor:
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0.163
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R-free:
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0.180
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Authors:
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L.P.Jackson,M.Lewis,H.M.Kent,M.A.Edeling,P.R.Evans,R.Duden,D.J.Owen
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Key ref:
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L.P.Jackson
et al.
(2012).
Molecular basis for recognition of dilysine trafficking motifs by COPI.
Dev Cell,
23,
1255-1262.
PubMed id:
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Date:
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17-Oct-12
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Release date:
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12-Dec-12
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PROCHECK
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Headers
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References
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P41811
(COPB2_YEAST) -
Coatomer subunit beta' from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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889 a.a.
300 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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Dev Cell
23:1255-1262
(2012)
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PubMed id:
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Molecular basis for recognition of dilysine trafficking motifs by COPI.
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L.P.Jackson,
M.Lewis,
H.M.Kent,
M.A.Edeling,
P.R.Evans,
R.Duden,
D.J.Owen.
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ABSTRACT
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COPI mediates retrograde trafficking from the Golgi to the endoplasmic reticulum
(ER) and within the Golgi stack, sorting transmembrane proteins bearing
C-terminal KKxx or KxKxx motifs. The structure of KxKxx motifs bound to the
N-terminal WD-repeat domain of β'-COP identifies electrostatic contacts between
the motif and complementary patches at the center of the β'-COP propeller. An
absolute requirement of a two-residue spacing between the terminal carboxylate
group and first lysine residue results from interactions of carbonyl groups in
the motif backbone with basic side chains of β'-COP. Similar interactions are
proposed to mediate binding of KKxx motifs by the homologous α-COP domain.
Mutation of key interacting residues in either domain or in their cognate motifs
abolishes in vitro binding and results in mistrafficking of dilysine-containing
cargo in yeast without compromising cell viability. Flexibility between β'-COP
WD-repeat domains and the location of cargo binding have implications for COPI
coat assembly.
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Links
