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PDBsum entry 3h8h
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Transcription
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PDB id
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3h8h
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Contents |
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* Residue conservation analysis
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PDB id:
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Transcription
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Title:
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Structure of thE C-terminal domain of human rnf2/ring1b;
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Structure:
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E3 ubiquitin-protein ligase ring2. Chain: a. Fragment: residues 220-330. Synonym: ring finger protein 2, ring finger protein 1b, ring1b, ring finger protein bap-1, ding protein, huntingtin-interacting protein 2- interacting protein 3, hip2-interacting protein 3. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: bap1, ding, hipi3, ring1b, rnf2. 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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0.202
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R-free:
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0.244
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Authors:
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J.R.Walker,I.Bezsonova,J.Bacik,S.Duan,J.Weigelt,C.Bountra, A.M.Edwards,C.H.Arrowsmith,A.Bochkarev,S.Dhe-Paganon,Structural Genomics Consortium (Sgc)
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Key ref:
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I.Bezsonova
et al.
(2009).
Ring1B contains a ubiquitin-like docking module for interaction with Cbx proteins.
Biochemistry,
48,
10542-10548.
PubMed id:
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Date:
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29-Apr-09
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Release date:
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23-Jun-09
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PROCHECK
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Headers
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References
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Q99496
(RING2_HUMAN) -
E3 ubiquitin-protein ligase RING2 from Homo sapiens
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Seq:
Struc:
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336 a.a.
92 a.a.
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Key: |
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Secondary structure |
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CATH domain |
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Enzyme class:
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E.C.2.3.2.27
- RING-type E3 ubiquitin transferase.
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Reaction:
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S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6- ubiquitinyl-[acceptor protein]-L-lysine
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Biochemistry
48:10542-10548
(2009)
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PubMed id:
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Ring1B contains a ubiquitin-like docking module for interaction with Cbx proteins.
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I.Bezsonova,
J.R.Walker,
J.P.Bacik,
S.Duan,
S.Dhe-Paganon,
C.H.Arrowsmith.
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ABSTRACT
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Polycomb group (PcG) proteins are a special set of repressive transcription
factors involved in epigenetic modifications of chromatin. They form two
functionally distinct groups of catalytically active complexes: Polycomb
repressive complex 1 (PRC1) and 2 (PRC2). The PRC1 complex is an important yet
poorly characterized multiprotein histone ubiquitylation machine responsible for
maintaining transcriptionally silent states of genes through histone H2A K119
modification. The Ring domain containing subunits of PRC1 also have
substrate-targeting domains that interact with Cbx proteins, which have been
implicated in chromatin and RNA binding. In this work, we present a high
resolution structure of the C-terminal domain of Ring1B, revealing a variant
ubiquitin-like fold with a distinct conserved surface region. On the basis of
crystal structure and mutational analysis of this domain we show that the
conserved surface is responsible for interaction with Cbx members of the PRC1
and homodimer formation. These data suggest a mechanism by which Ring1B serves
as an adaptor that mediates binding between the members of the PRC1 complex and
the nucleosome.
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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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A.Grzenda,
T.Ordog,
and
R.Urrutia
(2011).
Polycomb and the emerging epigenetics of pancreatic cancer.
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J Gastrointest Cancer,
42,
100-111.
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B.Demeler,
E.Brookes,
R.Wang,
V.Schirf,
and
C.A.Kim
(2010).
Characterization of reversible associations by sedimentation velocity with UltraScan.
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Macromol Biosci,
10,
775-782.
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J.M.Winget,
and
T.Mayor
(2010).
The diversity of ubiquitin recognition: hot spots and varied specificity.
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Mol Cell,
38,
627-635.
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R.Wang,
A.B.Taylor,
B.Z.Leal,
L.V.Chadwell,
U.Ilangovan,
A.K.Robinson,
V.Schirf,
P.J.Hart,
E.M.Lafer,
B.Demeler,
A.P.Hinck,
D.G.McEwen,
and
C.A.Kim
(2010).
Polycomb group targeting through different binding partners of RING1B C-terminal domain.
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Structure,
18,
966-975.
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PDB codes:
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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
codes are
shown on the right.
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Links
