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* Residue conservation analysis
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PDB id:
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Transferase
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Title:
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Methyltransferase domain of human suppressor of variegation 3-9 homolog 2
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Structure:
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Histone-lysine n-methyltransferase suv39h2. Chain: a. Fragment: methyltransferase domain: residues 112-410. Synonym: suppressor of variegation 3-9 homolog 2, su(var)3- 9 homolog 2, histone h3-k9 methyltransferase 2, h3-k9- hmtase 2. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: suv39h2. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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2.00Å
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R-factor:
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0.179
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R-free:
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0.213
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Authors:
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V.V.Lunin,H.Wu,H.Zeng,H.Ren,P.Loppnau,J.Weigelt,M.Sundstrom, C.H.Arrowsmith,A.M.Edwards,A.Bochkarev,A.N.Plotnikov,J.Min, Structural Genomics Consortium (Sgc)
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Key ref:
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H.Wu
et al.
(2010).
Structural biology of human H3K9 methyltransferases.
Plos One,
5,
e8570.
PubMed id:
DOI:
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Date:
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29-Aug-07
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Release date:
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11-Sep-07
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PROCHECK
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Headers
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References
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Q9H5I1
(SUV92_HUMAN) -
Histone-lysine N-methyltransferase SUV39H2
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Seq:
Struc:
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410 a.a.
270 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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Enzyme class:
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E.C.2.1.1.43
- Histone-lysine N-methyltransferase.
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Reaction:
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S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N6-methyl-L-lysine-[histone]
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S-adenosyl-L-methionine
Bound ligand (Het Group name = )
corresponds exactly
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L-lysine-[histone]
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=
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S-adenosyl-L-homocysteine
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N(6)-methyl-L-lysine-[histone]
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Gene Ontology (GO) functional annotation
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Cellular component
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nucleus
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1 term
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Biological process
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chromatin modification
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1 term
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Biochemical function
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zinc ion binding
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2 terms
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DOI no:
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Plos One
5:e8570
(2010)
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PubMed id:
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Structural biology of human H3K9 methyltransferases.
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H.Wu,
J.Min,
V.V.Lunin,
T.Antoshenko,
L.Dombrovski,
H.Zeng,
A.Allali-Hassani,
V.Campagna-Slater,
M.Vedadi,
C.H.Arrowsmith,
A.N.Plotnikov,
M.Schapira.
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ABSTRACT
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SET domain methyltransferases deposit methyl marks on specific histone tail
lysine residues and play a major role in epigenetic regulation of gene
transcription. We solved the structures of the catalytic domains of GLP, G9a,
Suv39H2 and PRDM2, four of the eight known human H3K9 methyltransferases in
their apo conformation or in complex with the methyl donating cofactor, and
peptide substrates. We analyzed the structural determinants for methylation
state specificity, and designed a G9a mutant able to tri-methylate H3K9. We show
that the I-SET domain acts as a rigid docking platform, while induced-fit of the
Post-SET domain is necessary to achieve a catalytically competent conformation.
We also propose a model where long-range electrostatics bring enzyme and histone
substrate together, while the presence of an arginine upstream of the target
lysine is critical for binding and specificity. ENHANCED VERSION: This article
can also be viewed as an enhanced version in which the text of the article is
integrated with interactive 3D representations and animated transitions. Please
note that a web plugin is required to access this enhanced functionality.
Instructions for the installation and use of the web plugin are available in
Text S1.
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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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D.B.Yap,
J.Chu,
T.Berg,
M.Schapira,
S.W.Cheng,
A.Moradian,
R.D.Morin,
A.J.Mungall,
B.Meissner,
M.Boyle,
V.E.Marquez,
M.A.Marra,
R.D.Gascoyne,
R.K.Humphries,
C.H.Arrowsmith,
G.B.Morin,
and
S.A.Aparicio
(2011).
Somatic mutations at EZH2 Y641 act dominantly through a mechanism of selectively altered PRC2 catalytic activity, to increase H3K27 trimethylation.
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Blood, 117,
2451-2459.
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V.Hoppmann,
T.Thorstensen,
P.E.Kristiansen,
S.V.Veiseth,
M.A.Rahman,
K.Finne,
R.B.Aalen,
and
R.Aasland
(2011).
The CW domain, a new histone recognition module in chromatin proteins.
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EMBO J, 30,
1939-1952.
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PDB code:
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C.J.Sneeringer,
M.P.Scott,
K.W.Kuntz,
S.K.Knutson,
R.M.Pollock,
V.M.Richon,
and
R.A.Copeland
(2010).
Coordinated activities of wild-type plus mutant EZH2 drive tumor-associated hypertrimethylation of lysine 27 on histone H3 (H3K27) in human B-cell lymphomas.
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Proc Natl Acad Sci U S A, 107,
20980-20985.
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T.J.Wigle,
L.M.Provencher,
J.L.Norris,
J.Jin,
P.J.Brown,
S.V.Frye,
and
W.P.Janzen
(2010).
Accessing protein methyltransferase and demethylase enzymology using microfluidic capillary electrophoresis.
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Chem Biol, 17,
695-704.
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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.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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Links
