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PDBsum entry 4w5a
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Hydrolase/structural protein
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PDB id
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4w5a
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Contents |
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128 a.a.
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11 a.a.
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12 a.a.
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114 a.a.
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PDB id:
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| Name: |
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Hydrolase/structural protein
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Title:
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Complex structure of atrx add bound to h3k9me3s10ph peptide
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Structure:
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Transcriptional regulator atrx. Chain: a, b, e. Fragment: unp residues 167-289. Synonym: atp-dependent helicase atrx,x-linked helicase ii,x-linked nuclear protein,xnp,znf-hx. Engineered: yes. Mutation: yes. Peptide from histone h3.3. Chain: c, d, f.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: atrx, rad54l, xh2. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Organism_taxid: 9606
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Resolution:
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2.60Å
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R-factor:
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0.224
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R-free:
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0.260
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Authors:
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D.Zhao,B.Xiang,H.Li
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Key ref:
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K.M.Noh
et al.
(2015).
ATRX tolerates activity-dependent histone H3 methyl/phos switching to maintain repetitive element silencing in neurons.
Proc Natl Acad Sci U S A,
112,
6820-6827.
PubMed id:
DOI:
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Date:
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17-Aug-14
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Release date:
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21-Jan-15
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PROCHECK
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Headers
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References
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P46100
(ATRX_HUMAN) -
Transcriptional regulator ATRX from Homo sapiens
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Seq:
Struc:
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2492 a.a.
128 a.a.*
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P84243
(H33_HUMAN) -
Histone H3.3 from Homo sapiens
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Seq:
Struc:
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136 a.a.
11 a.a.*
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Enzyme class:
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Chains A, B, E:
E.C.3.6.4.12
- Dna helicase.
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Reaction:
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ATP + H2O = ADP + phosphate + H+
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ATP
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+
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H2O
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=
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ADP
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+
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phosphate
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+
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H(+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Proc Natl Acad Sci U S A
112:6820-6827
(2015)
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PubMed id:
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ATRX tolerates activity-dependent histone H3 methyl/phos switching to maintain repetitive element silencing in neurons.
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K.M.Noh,
I.Maze,
D.Zhao,
B.Xiang,
W.Wenderski,
P.W.Lewis,
L.Shen,
H.Li,
C.D.Allis.
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ABSTRACT
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ATRX (the alpha thalassemia/mental retardation syndrome X-linked protein) is a
member of the switch2/sucrose nonfermentable2 (SWI2/SNF2) family of
chromatin-remodeling proteins and primarily functions at heterochromatic loci
via its recognition of "repressive" histone modifications [e.g.,
histone H3 lysine 9 tri-methylation (H3K9me3)]. Despite significant roles for
ATRX during normal neural development, as well as its relationship to human
disease, ATRX function in the central nervous system is not well understood.
Here, we describe ATRX's ability to recognize an activity-dependent
combinatorial histone modification, histone H3 lysine 9 tri-methylation/serine
10 phosphorylation (H3K9me3S10ph), in postmitotic neurons. In neurons, this
"methyl/phos" switch occurs exclusively after periods of stimulation
and is highly enriched at heterochromatic repeats associated with centromeres.
Using a multifaceted approach, we reveal that H3K9me3S10ph-bound Atrx represses
noncoding transcription of centromeric minor satellite sequences during
instances of heightened activity. Our results indicate an essential interaction
between ATRX and a previously uncharacterized histone modification in the
central nervous system and suggest a potential role for abnormal repetitive
element transcription in pathological states manifested by ATRX dysfunction.
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