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PDBsum entry 4n5a
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Protein binding
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PDB id
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4n5a
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PDB id:
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| Name: |
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Protein binding
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Title:
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Crystal structure of efr3
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Structure:
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Protein efr3. Chain: a. Fragment: residues 8-562. Engineered: yes
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Source:
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Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 559292. Strain: atcc 204508 / s288c. Gene: efr3, ymr212c, ym8261.06c. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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3.20Å
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R-factor:
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0.232
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R-free:
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0.256
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Authors:
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X.Wu,R.J.Chi,J.M.Baskin,L.Lucast,C.G.Burd,P.De Camilli,K.M.Reinisch
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Key ref:
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X.Wu
et al.
(2014).
Structural insights into assembly and regulation of the plasma membrane phosphatidylinositol 4-kinase complex.
Dev Cell,
28,
19-29.
PubMed id:
DOI:
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Date:
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09-Oct-13
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Release date:
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22-Jan-14
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PROCHECK
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Headers
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References
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Q03653
(EFR3_YEAST) -
Protein EFR3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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782 a.a.
535 a.a.
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DOI no:
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Dev Cell
28:19-29
(2014)
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PubMed id:
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Structural insights into assembly and regulation of the plasma membrane phosphatidylinositol 4-kinase complex.
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X.Wu,
R.J.Chi,
J.M.Baskin,
L.Lucast,
C.G.Burd,
P.De Camilli,
K.M.Reinisch.
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ABSTRACT
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Plasma membrane PI4P helps determine the identity of this membrane and plays a
key role in signal transduction as the precursor of PI(4,5)P2 and its
metabolites. Here, we report the atomic structure of the protein scaffold that
is required for the plasma membrane localization and function of Stt4/PI4KIIIα,
the PI 4-kinase responsible for this PI4P pool. Both proteins of the scaffold,
Efr3 and YPP1/TTC7, are composed of α-helical repeats, which are arranged into
a rod in Efr3 and a superhelix in Ypp1. A conserved basic patch in Efr3, which
binds acidic phospholipids, anchors the complex to the plasma membrane.
Stt4/PI4KIIIα is recruited by interacting with the Ypp1 C-terminal lobe, which
also binds to unstructured regions in the Efr3 C terminus. Phosphorylation of
this Efr3 region counteracts Ypp1 binding, thus providing a mechanism through
which Stt4/PI4KIIIα recruitment, and thus a metabolic reaction of fundamental
importance in cell physiology, can be regulated.
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Links
