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PDBsum entry 5udh
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411 a.a.
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152 a.a.
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381 a.a.
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73 a.a.
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PDB id:
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| Name: |
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Transferase
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Title:
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Hhari/arih1-ubch7~ubiquitin
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Structure:
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E3 ubiquitin-protein ligase arih1. Chain: a, b. Fragment: unp residues 90-557. Synonym: h7-ap2,hhari,monocyte protein 6,mop-6,protein ariadne-1 homolog,ari-1,ubch7-binding protein,ubcm4-interacting protein, ubiquitin-conjugating enzyme e2-binding protein 1. Engineered: yes. Ubiquitin-conjugating enzyme e2 l3. Chain: c, d.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: arih1, ari, mop6, ubch7bp, hussy-27. Expressed in: escherichia coli-pichia pastoris shuttle vector ppparg4. Expression_system_taxid: 1182032. Gene: ube2l3, ubce7, ubch7. Expression_system_taxid: 1182032
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Resolution:
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3.24Å
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R-factor:
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0.225
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R-free:
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0.279
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Authors:
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D.J.Miller,B.A.Schulman
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Key ref:
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K.K.Dove
et al.
(2017).
Structural Studies of HHARI/UbcH7∼Ub Reveal Unique E2∼Ub Conformational Restriction by RBR RING1.
Structure,
25,
890.
PubMed id:
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Date:
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27-Dec-16
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Release date:
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14-Jun-17
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PROCHECK
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Headers
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References
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Q9Y4X5
(ARI1_HUMAN) -
E3 ubiquitin-protein ligase ARIH1 from Homo sapiens
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Seq:
Struc:
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557 a.a.
411 a.a.
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P68036
(UB2L3_HUMAN) -
Ubiquitin-conjugating enzyme E2 L3 from Homo sapiens
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Seq:
Struc:
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154 a.a.
152 a.a.*
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Enzyme class 2:
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Chains A, B:
E.C.2.3.2.31
- RBR-type E3 ubiquitin transferase.
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Reaction:
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[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine
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Enzyme class 3:
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Chains C, D:
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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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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Structure
25:890
(2017)
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PubMed id:
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Structural Studies of HHARI/UbcH7∼Ub Reveal Unique E2∼Ub Conformational Restriction by RBR RING1.
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K.K.Dove,
J.L.Olszewski,
L.Martino,
D.M.Duda,
X.S.Wu,
D.J.Miller,
K.H.Reiter,
K.Rittinger,
B.A.Schulman,
R.E.Klevit.
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ABSTRACT
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RING-between-RING (RBR) E3s contain RING1 domains that are structurally similar
yet mechanistically distinct from canonical RING domains. Both types of E3 bind
E2∼ubiquitin (E2∼Ub) via their RINGs but canonical RING E3s promote closed
E2∼Ub conformations required for direct Ub transfer from the E2 to substrate,
while RBR RING1s promote open E2∼Ub to favor Ub transfer to the E3 active
site. This different RING/E2∼Ub conformation determines its direct target,
which for canonical RING E3s is typically a substrate or substrate-linked Ub,
but is the E3 active-site cysteine in the case of RBR-type E3s. Here we show
that a short extension of HHARI RING1, namely Zn2+-loop II, not
present in any RING E3s, acts as a steric wedge to disrupt closed E2∼Ub,
providing a structural explanation for the distinctive RING1-dependent
conformational restriction mechanism utilized by RBR E3s.
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