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PDBsum entry 2ln0
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PDB id:
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Transferase
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Title:
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Structure of moz
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Structure:
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Histone acetyltransferase kat6a. Chain: a. Fragment: unp residues 204-313. Synonym: moz, ybf2/sas3, sas2 and tip60 protein 3, myst-3, monocytic leukemia zinc finger protein, runt-related transcription factor- binding protein 2, zinc finger protein 220. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: kat6a, moz, myst3, runxbp2, znf220. Expressed in: escherichia coli. Expression_system_taxid: 562.
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NMR struc:
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20 models
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Authors:
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Y.Qiu
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Key ref:
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Y.Qiu
et al.
(2012).
Combinatorial readout of unmodified H3R2 and acetylated H3K14 by the tandem PHD finger of MOZ reveals a regulatory mechanism for HOXA9 transcription.
Genes Dev,
26,
1376-1391.
PubMed id:
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Date:
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15-Dec-11
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Release date:
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27-Jun-12
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PROCHECK
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Headers
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References
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Q92794
(KAT6A_HUMAN) -
Histone acetyltransferase KAT6A from Homo sapiens
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Seq:
Struc:
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2004 a.a.
110 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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Enzyme class:
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E.C.2.3.1.48
- histone acetyltransferase.
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Reaction:
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L-lysyl-[protein] + acetyl-CoA = N6-acetyl-L-lysyl-[protein] + CoA + H+
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L-lysyl-[protein]
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+
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acetyl-CoA
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=
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N(6)-acetyl-L-lysyl-[protein]
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+
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CoA
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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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Genes Dev
26:1376-1391
(2012)
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PubMed id:
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Combinatorial readout of unmodified H3R2 and acetylated H3K14 by the tandem PHD finger of MOZ reveals a regulatory mechanism for HOXA9 transcription.
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Y.Qiu,
L.Liu,
C.Zhao,
C.Han,
F.Li,
J.Zhang,
Y.Wang,
G.Li,
Y.Mei,
M.Wu,
J.Wu,
Y.Shi.
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ABSTRACT
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Histone acetylation is a hallmark for gene transcription. As a histone
acetyltransferase, MOZ (monocytic leukemia zinc finger protein) is important for
HOX gene expression as well as embryo and postnatal development. In vivo, MOZ
forms a tetrameric complex with other subunits, including several
chromatin-binding modules with regulatory functions. Here we report the solution
structure of the tandem PHD (plant homeodomain) finger (PHD12) of human MOZ in a
free state and the 1.47 Å crystal structure in complex with H3K14ac peptide,
which reveals the structural basis for the recognition of unmodified R2 and
acetylated K14 on histone H3. Moreover, the results of chromatin
immunoprecipitation (ChIP) and RT-PCR assays indicate that PHD12 facilitates the
localization of MOZ onto the promoter locus of the HOXA9 gene, thereby promoting
the H3 acetylation around the promoter region and further up-regulating the
HOXA9 mRNA level. Taken together, our findings suggest that the combinatorial
readout of the H3R2/K14ac by PHD12 might represent an important epigenetic
regulatory mechanism that governs transcription and also provide a clue of
cross-talk between the MOZ complex and histone H3 modifications.
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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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C.A.Musselman,
M.E.Lalonde,
J.Côté,
and
T.G.Kutateladze
(2012).
Perceiving the epigenetic landscape through histone readers.
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Nat Struct Mol Biol,
19,
1218-1227.
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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
