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PDBsum entry 1zgu
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Ligase/signaling protein
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PDB id
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1zgu
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Contents |
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* Residue conservation analysis
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PDB id:
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Ligase/signaling protein
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Title:
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Solution structure of the human mms2-ubiquitin complex
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Structure:
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Ubiquitin-conjugating enzyme e2 variant 2. Chain: a. Synonym: mms2, enterocyte differentiation associated factor edaf-1, enterocyte differentiation promoting factor, edpf-1, vitamin d3 inducible protein, ddvit 1. Engineered: yes. Ubiquitin. Chain: b. Engineered: yes.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: ube2v2, mms2. Expressed in: escherichia coli. Expression_system_taxid: 562.
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NMR struc:
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10 models
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Authors:
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M.J.Lewis,L.F.Saltibus,D.D.Hau,W.Xiao,L.Spyracopoulos
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Key ref:
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M.J.Lewis
et al.
(2006).
Structural basis for non-covalent interaction between ubiquitin and the ubiquitin conjugating enzyme variant human MMS2.
J Biomol Nmr,
34,
89.
PubMed id:
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Date:
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22-Apr-05
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Release date:
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04-Apr-06
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PROCHECK
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Headers
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References
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Enzyme class:
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Chains A, B:
E.C.?
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J Biomol Nmr
34:89
(2006)
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PubMed id:
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Structural basis for non-covalent interaction between ubiquitin and the ubiquitin conjugating enzyme variant human MMS2.
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M.J.Lewis,
L.F.Saltibus,
D.D.Hau,
W.Xiao,
L.Spyracopoulos.
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ABSTRACT
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Modification of proteins by post-translational covalent attachment of a single,
or chain, of ubiquitin molecules serves as a signaling mechanism for a number of
regulatory functions in eukaryotic cells. For example, proteins tagged with
lysine-63 linked polyubiquitin chains are involved in error-free DNA repair. The
catalysis of lysine-63 linked polyubiquitin chains involves the sequential
activity of three enzymes (E1, E2, and E3) that ultimately transfer a ubiquitin
thiolester intermediate to a protein target. The E2 responsible for catalysis of
lysine-63 linked polyubiquitination is a protein heterodimer consisting of a
canonical E2 known as Ubc13, and an E2-like protein, or ubiquitin conjugating
enzyme variant (UEV), known as Mms2. We have determined the solution structure
of the complex formed by human Mms2 and ubiquitin using high resolution,
solution state nuclear magnetic resonance (NMR) spectroscopy. The structure of
the Mms2-Ub complex provides important insights into the molecular basis
underlying the catalysis of lysine-63 linked polyubiquitin chains.
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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.R.Cole,
L.P.Lewis,
and
H.Walden
(2010).
The structure of the catalytic subunit FANCL of the Fanconi anemia core complex.
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Nat Struct Mol Biol,
17,
294-298.
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PDB code:
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D.M.Wenzel,
K.E.Stoll,
and
R.E.Klevit
(2010).
E2s: structurally economical and functionally replete.
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Biochem J,
433,
31-42.
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F.Zhou
(2009).
Molecular mechanisms of viral immune evasion proteins to inhibit MHC class I antigen processing and presentation.
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Int Rev Immunol,
28,
376-393.
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C.T.Jurgenson,
K.E.Burns,
T.P.Begley,
and
S.E.Ealick
(2008).
Crystal structure of a sulfur carrier protein complex found in the cysteine biosynthetic pathway of Mycobacterium tuberculosis.
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Biochemistry,
47,
10354-10364.
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PDB codes:
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M.V.Poyurovsky,
C.Priest,
A.Kentsis,
K.L.Borden,
Z.Q.Pan,
N.Pavletich,
and
C.Prives
(2007).
The Mdm2 RING domain C-terminus is required for supramolecular assembly and ubiquitin ligase activity.
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EMBO J,
26,
90.
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P.Knipscheer,
W.J.van Dijk,
J.V.Olsen,
M.Mann,
and
T.K.Sixma
(2007).
Noncovalent interaction between Ubc9 and SUMO promotes SUMO chain formation.
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EMBO J,
26,
2797-2807.
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PDB code:
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P.Mercier,
M.J.Lewis,
D.D.Hau,
L.F.Saltibus,
W.Xiao,
and
L.Spyracopoulos
(2007).
Structure, interactions, and dynamics of the RING domain from human TRAF6.
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Protein Sci,
16,
602-614.
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PDB code:
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M.J.Eddins,
C.M.Carlile,
K.M.Gomez,
C.M.Pickart,
and
C.Wolberger
(2006).
Mms2-Ubc13 covalently bound to ubiquitin reveals the structural basis of linkage-specific polyubiquitin chain formation.
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Nat Struct Mol Biol,
13,
915-920.
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PDB code:
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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
