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PDBsum entry 4z4p
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PDB id:
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Transferase
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Title:
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Structure of the mll4 set domain
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Structure:
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Histone-lysine n-methyltransferase 2d. Chain: a. Fragment: unp residues 5385-5539. Synonym: lysine n-methyltransferase 2d,all1-related protein, myeloid/lymphoid or mixed-lineage leukemia protein 2. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: kmt2d, alr, mll2, mll4. Expressed in: escherichia coli #1/h766. Expression_system_taxid: 1354003
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Resolution:
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2.20Å
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R-factor:
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0.196
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R-free:
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0.242
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Authors:
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Z.Zhang,A.Mittal,J.Reid,S.Reich,S.J.Gamblin,J.R.Wilson
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Key ref:
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Y.Zhang
et al.
(2015).
Evolving Catalytic Properties of the MLL Family SET Domain.
Structure,
23,
1921-1933.
PubMed id:
DOI:
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Date:
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02-Apr-15
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Release date:
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09-Sep-15
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PROCHECK
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Headers
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References
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O14686
(KMT2D_HUMAN) -
Histone-lysine N-methyltransferase 2D from Homo sapiens
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Seq:
Struc:
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5537 a.a.
161 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.2.1.1.364
- [histone H3]-lysine(4) N-methyltransferase.
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Reaction:
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L-lysyl4-[histone H3] + S-adenosyl-L-methionine = N6-methyl-L- lysyl4-[histone H3] + S-adenosyl-L-homocysteine + H+
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L-lysyl(4)-[histone H3]
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+
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S-adenosyl-L-methionine
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=
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N(6)-methyl-L- lysyl(4)-[histone H3]
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+
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S-adenosyl-L-homocysteine
Bound ligand (Het Group name = )
corresponds exactly
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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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Structure
23:1921-1933
(2015)
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PubMed id:
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Evolving Catalytic Properties of the MLL Family SET Domain.
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Y.Zhang,
A.Mittal,
J.Reid,
S.Reich,
S.J.Gamblin,
J.R.Wilson.
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ABSTRACT
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Methylation of histone H3 lysine-4 is a hallmark of chromatin associated with
active gene expression. The activity of H3K4-specific modification enzymes, in
higher eukaryotes the MLL (or KMT2) family, is tightly regulated. The MLL family
has six members, each with a specialized function. All contain a catalytic SET
domain that associates with a core multiprotein complex for activation. These
SET domains segregate into three classes that correlate with the arrangement of
targeting domains that populate the rest of the protein. Here we show that,
unlike MLL1, the MLL4 SET domain retains significant activity without the core
complex. We also present the crystal structure of an inactive MLL4-tagged SET
domain construct and describe conformational changes that account for MLL4
intrinsic activity. Finally, our structure explains how the MLL SET domains are
able to add multiple methyl groups to the target lysine, despite having the
sequence characteristics of a classical monomethylase.
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Links
