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PDBsum entry 3odt
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Nuclear protein
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PDB id
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3odt
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Nuclear protein
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Title:
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Crystal structure of wd40 beta propeller domain of doa1
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Structure:
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Protein doa1. Chain: a, b. Fragment: wd40 beta propeller domain. Engineered: yes
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Source:
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Saccharomyces cerevisiae. Yeast. Organism_taxid: 4932. Gene: doa1, ufd3, zzz4, ykl213c. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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1.35Å
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R-factor:
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0.139
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R-free:
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0.176
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Authors:
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N.Pashkova,L.Gakhar,S.C.Winistorfer,L.Yu,S.Ramaswamy,R.C.Piper
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Key ref:
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N.Pashkova
et al.
(2010).
WD40 repeat propellers define a ubiquitin-binding domain that regulates turnover of F box proteins.
Mol Cell,
40,
433-443.
PubMed id:
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Date:
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11-Aug-10
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Release date:
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01-Dec-10
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PROCHECK
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Headers
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References
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P36037
(DOA1_YEAST) -
Protein DOA1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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715 a.a.
296 a.a.*
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Key: |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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Mol Cell
40:433-443
(2010)
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PubMed id:
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WD40 repeat propellers define a ubiquitin-binding domain that regulates turnover of F box proteins.
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N.Pashkova,
L.Gakhar,
S.C.Winistorfer,
L.Yu,
S.Ramaswamy,
R.C.Piper.
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ABSTRACT
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WD40-repeat β-propellers are found in a wide range of proteins involved in
distinct biological activities. We define a large subset of WD40 β-propellers
as a class of ubiquitin-binding domains. Using the β-propeller from Doa1/Ufd3
as a paradigm, we find the conserved top surface of the Doa1 β-propeller binds
the hydrophobic patch of ubiquitin centered on residues I44, L8, and V70.
Mutations that disrupt ubiquitin binding abrogate Doa1 function, demonstrating
the importance of this interaction. We further demonstrate that WD40
β-propellers from a functionally diverse set of proteins bind ubiquitin in a
similar fashion. This set includes members of the F box family of SCF ubiquitin
E3 ligase adaptors. Using mutants defective in binding, we find that ubiquitin
interaction by the F box protein Cdc4 promotes its autoubiquitination and
turnover. Collectively, our results reveal a molecular mechanism that may
account for how ubiquitin controls a broad spectrum of cellular activities.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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H.Davis,
A.Lewis,
B.Spencer-Dene,
H.Tateossian,
G.Stamp,
A.Behrens,
and
I.Tomlinson
(2011).
FBXW7 mutations typically found in human cancers are distinct from null alleles and disrupt lung development.
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J Pathol,
224,
180-189.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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Links
