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PDBsum entry 3t6r
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Transcription
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PDB id
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3t6r
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PDB id:
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| Name: |
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Transcription
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Title:
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Structure of uhrf1 in complex with unmodified h3 n-terminal tail
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Structure:
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E3 ubiquitin-protein ligase uhrf1. Chain: a, b. Fragment: unp residues 299-364. Synonym: inverted ccaat box-binding protein of 90 kda, nuclear protein 95, nuclear zinc finger protein np95, hunp95, ring finger protein 106, transcription factor icbp90, ubiquitin-like phd and ring finger domain-containing protein 1, ubiquitin-like-containing phd and ring finger domains protein 1. Engineered: yes.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Organism_taxid: 9606
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Resolution:
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1.95Å
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R-factor:
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0.195
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R-free:
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0.229
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Authors:
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S.Xie,J.Jakoncic,C.M.Qian
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Key ref:
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S.Xie
et al.
(2012).
UHRF1 double tudor domain and the adjacent PHD finger act together to recognize K9me3-containing histone H3 tail.
J Mol Biol,
415,
318-328.
PubMed id:
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Date:
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29-Jul-11
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Release date:
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23-Nov-11
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PROCHECK
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Headers
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References
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Q96T88
(UHRF1_HUMAN) -
E3 ubiquitin-protein ligase UHRF1 from Homo sapiens
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Seq:
Struc:
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793 a.a.
70 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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*
PDB and UniProt seqs differ
at 4 residue positions (black
crosses)
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Enzyme class:
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E.C.2.3.2.27
- RING-type E3 ubiquitin transferase.
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Reaction:
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S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6- ubiquitinyl-[acceptor protein]-L-lysine
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J Mol Biol
415:318-328
(2012)
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PubMed id:
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UHRF1 double tudor domain and the adjacent PHD finger act together to recognize K9me3-containing histone H3 tail.
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S.Xie,
J.Jakoncic,
C.Qian.
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ABSTRACT
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Human multi-domain-containing protein UHRF1 has recently been extensively
characterized as a key epigenetic regulator for maintaining DNA methylation
patterns. UHRF1 SRA domain preferentially binds to hemimethylated CpG sites, and
double Tudor domain has been implicated in recognizing H3K9me3 mark, but the
role of the adjacent PHD finger remains unclear. Here, we report the
high-resolution crystal structure of UHRF1 PHD finger in complex with N-terminal
tail of histone H3. We found that the preceding zinc-Cys4 knuckle is
indispensable for the PHD finger of UHRF1 to recognize the first four unmodified
residues of histone H3 N-terminal tail. Quantitative binding studies indicated
that UHRF1 PHD finger (including the preceding zinc-Cys4 knuckle) acts together
with the adjacent double Tudor domain to specifically recognize the H3K9me3
mark. Combinatorial recognition of H3K9me3-containing histone H3 tail by UHRF1
PHD finger and double Tudor domain may play a role in establishing and
maintaining histone H3K9 methylation patterns during the cell cycle.
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Links
