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PDBsum entry 4ddi
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Hydrolase/ligase
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PDB id
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4ddi
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Contents |
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399 a.a.
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(+ 0 more)
76 a.a.
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PDB id:
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| Name: |
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Hydrolase/ligase
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Title:
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Crystal structure of human otub1/ubch5b~ub/ub
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Structure:
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Ubiquitin-conjugating enzyme e2 d2, ubiquitin thioesterase otub1. Chain: a, b, c. Synonym: ubiquitin carrier protein d2, ubiquitin-conjugating enzyme e2(17)kb 2, ubiquitin-conjugating enzyme e2-17 kda 2, ubiquitin- protein ligase d2, deubiquitinating enzyme otub1, otu domain- containing ubiquitin aldehyde-binding protein 1, otubain-1, hotu1, ubiquitin-specific-processing protease otub1. Engineered: yes.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: ube2d2, ubc4, ubc5b, ubch4, ubch5b, hspc263, otb1, otu1, otub1. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: ubc. Expression_system_taxid: 562
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Resolution:
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3.80Å
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R-factor:
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0.221
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R-free:
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0.273
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Authors:
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Y.C.Juang,M.Sanches,F.Sicheri
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Key ref:
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Y.C.Juang
et al.
(2012).
OTUB1 co-opts Lys48-linked ubiquitin recognition to suppress E2 enzyme function.
Mol Cell,
45,
384-397.
PubMed id:
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Date:
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18-Jan-12
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Release date:
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22-Feb-12
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PROCHECK
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Headers
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References
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P62837
(UB2D2_HUMAN) -
Ubiquitin-conjugating enzyme E2 D2 from Homo sapiens
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Seq:
Struc:
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147 a.a.
399 a.a.*
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Enzyme class 2:
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Chains A, B, C:
E.C.2.3.2.23
- E2 ubiquitin-conjugating enzyme.
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Reaction:
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L- cysteine
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Enzyme class 3:
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Chains A, B, C:
E.C.2.3.2.24
- (E3-independent) E2 ubiquitin-conjugating enzyme.
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Reaction:
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + N6- monoubiquitinyl-[acceptor protein]-L-lysine
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Enzyme class 4:
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Chains A, B, C:
E.C.3.4.19.12
- ubiquitinyl hydrolase 1.
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Reaction:
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Thiol-dependent hydrolysis of ester, thiolester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
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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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Mol Cell
45:384-397
(2012)
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PubMed id:
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OTUB1 co-opts Lys48-linked ubiquitin recognition to suppress E2 enzyme function.
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Y.C.Juang,
M.C.Landry,
M.Sanches,
V.Vittal,
C.C.Leung,
D.F.Ceccarelli,
A.R.Mateo,
J.N.Pruneda,
D.Y.Mao,
R.K.Szilard,
S.Orlicky,
M.Munro,
P.S.Brzovic,
R.E.Klevit,
F.Sicheri,
D.Durocher.
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ABSTRACT
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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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Y.Ye,
G.Blaser,
M.H.Horrocks,
M.J.Ruedas-Rama,
S.Ibrahim,
A.A.Zhukov,
A.Orte,
D.Klenerman,
S.E.Jackson,
and
D.Komander
(2012).
Ubiquitin chain conformation regulates recognition and activity of interacting proteins.
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Nature,
492,
266-270.
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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.
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Links
