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PDBsum entry 5f6l
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Protein binding/transferase
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PDB id
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5f6l
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Contents |
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19 a.a.
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178 a.a.
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153 a.a.
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PDB id:
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| Name: |
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Protein binding/transferase
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Title:
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The crystal structure of mll1 (n3861i/q3867l) in complex with rbbp5 and ash2l
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Structure:
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Retinoblastoma-binding protein 5. Chain: j. Fragment: unp residues 330-356. Synonym: rbbp-5,retinoblastoma-binding protein rbq-3. Engineered: yes. Set1/ash2 histone methyltransferase complex subunit ash2. Chain: b. Fragment: unp residues 380-496, 539-598. Synonym: ash2-like protein.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: rbbp5, rbq3. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: ash2l, ash2l1. Gene: kmt2a, all1, cxxc7, hrx, htrx, mll, mll1, trx1.
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Resolution:
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1.90Å
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R-factor:
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0.171
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R-free:
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0.213
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Authors:
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Y.Li,M.Lei,Y.Chen
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Key ref:
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Y.Li
et al.
(2016).
Structural basis for activity regulation of MLL family methyltransferases.
Nature,
530,
447-452.
PubMed id:
DOI:
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Date:
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06-Dec-15
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Release date:
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24-Feb-16
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PROCHECK
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Headers
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References
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Q15291
(RBBP5_HUMAN) -
Retinoblastoma-binding protein 5 from Homo sapiens
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Seq:
Struc:
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538 a.a.
19 a.a.
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Enzyme class 1:
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Chain A:
E.C.2.1.1.-
- ?????
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Enzyme class 2:
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Chain A:
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
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+
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H(+)
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Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
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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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Nature
530:447-452
(2016)
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PubMed id:
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Structural basis for activity regulation of MLL family methyltransferases.
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Y.Li,
J.Han,
Y.Zhang,
F.Cao,
Z.Liu,
S.Li,
J.Wu,
C.Hu,
Y.Wang,
J.Shuai,
J.Chen,
L.Cao,
D.Li,
P.Shi,
C.Tian,
J.Zhang,
Y.Dou,
G.Li,
Y.Chen,
M.Lei.
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ABSTRACT
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The mixed lineage leukaemia (MLL) family of proteins (including MLL1-MLL4, SET1A
and SET1B) specifically methylate histone 3 Lys4, and have pivotal roles in the
transcriptional regulation of genes involved in haematopoiesis and development.
The methyltransferase activity of MLL1, by itself severely compromised, is
stimulated by the three conserved factors WDR5, RBBP5 and ASH2L, which are
shared by all MLL family complexes. However, the molecular mechanism of how
these factors regulate the activity of MLL proteins still remains poorly
understood. Here we show that a minimized human RBBP5-ASH2L heterodimer is the
structural unit that interacts with and activates all MLL family histone
methyltransferases. Our structural, biochemical and computational analyses
reveal a two-step activation mechanism of MLL family proteins. These findings
provide unprecedented insights into the common theme and functional plasticity
in complex assembly and activity regulation of MLL family methyltransferases,
and also suggest a universal regulation mechanism for most histone
methyltransferases.
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Links
