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PDBsum entry 3zkj
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Transcription
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PDB id
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3zkj
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Contents |
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257 a.a.
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82 a.a.
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70 a.a.
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105 a.a.
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PDB id:
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Transcription
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Title:
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Crystal structure of ankyrin repeat and socs box-containing protein 9 (asb9) in complex with elonginb and elonginc
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Structure:
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Ankyrin repeat and socs box protein 9. Chain: a, d. Fragment: residues 35-294. Synonym: asb-9. Engineered: yes. Transcription elongation factor b polypeptide 1. Chain: b, e. Fragment: residues 17-112. Synonym: RNA polymerase ii transcription factor, eloc, siii subunit
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Organ: kidney. Expressed in: escherichia coli. Expression_system_taxid: 511693.
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Resolution:
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2.58Å
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R-factor:
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0.229
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R-free:
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0.265
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Authors:
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J.R.C.Muniz,K.Guo,Y.Zhang,V.Ayinampudi,P.Savitsky,T.Keates, P.Filippakopoulos,M.Vollmar,W.W.Yue,T.Krojer,E.Ugochukwu,F.Von Delft,S.Knapp,J.Weigelt,C.H.Arrowsmith,A.M.Edwards,C.Bountra, A.N.Bullock
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Key ref:
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J.R.Muniz
et al.
(2013).
Molecular architecture of the ankyrin SOCS box family of Cul5-dependent E3 ubiquitin ligases.
J Mol Biol,
425,
3166-3177.
PubMed id:
DOI:
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Date:
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23-Jan-13
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Release date:
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30-Jan-13
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Supersedes:
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PROCHECK
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Headers
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References
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Q96DX5
(ASB9_HUMAN) -
Ankyrin repeat and SOCS box protein 9 from Homo sapiens
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Seq:
Struc:
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294 a.a.
257 a.a.
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Q15369
(ELOC_HUMAN) -
Elongin-C from Homo sapiens
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Seq:
Struc:
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112 a.a.
82 a.a.
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Enzyme class:
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Chains A, B, C, D, E, F:
E.C.?
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DOI no:
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J Mol Biol
425:3166-3177
(2013)
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PubMed id:
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Molecular architecture of the ankyrin SOCS box family of Cul5-dependent E3 ubiquitin ligases.
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J.R.Muniz,
K.Guo,
N.J.Kershaw,
V.Ayinampudi,
F.von Delft,
J.J.Babon,
A.N.Bullock.
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ABSTRACT
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Multi-subunit Cullin-RING E3 ligases often use repeat domain proteins as
substrate-specific adaptors. Structures of these macromolecular assemblies are
determined for the F-box-containing leucine-rich repeat and WD40 repeat
families, but not for the suppressor of cytokine signaling (SOCS)-box-containing
ankyrin repeat proteins (ASB1-18), which assemble with Elongins B and C and
Cul5. We determined the crystal structures of the ternary complex of
ASB9-Elongin B/C as well as the interacting N-terminal domain of Cul5 and used
structural comparisons to establish a model for the complete Cul5-based E3
ligase. The structures reveal a distinct architecture of the ASB9 complex that
positions the ankyrin domain coaxial to the SOCS box-Elongin B/C complex and
perpendicular to other repeat protein complexes. This alternative architecture
appears favorable to present the ankyrin domain substrate-binding site to the
E2-ubiquitin, while also providing spacing suitable for bulky ASB9 substrates,
such as the creatine kinases. The presented Cul5 structure also differs from
previous models and deviates from other Cullins via a rigid-body rotation
between Cullin repeats. This work highlights the adaptability of repeat domain
proteins as scaffolds in substrate recognition and lays the foundation for
future structure-function studies of this important E3 family.
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