5UDH

HHARI/ARIH1-UBCH7~Ubiquitin

Summary for 5UDH

• Entry DOI: 10.2210/pdb5udh/pdb
• Descriptor: E3 ubiquitin-protein ligase ARIH1, Ubiquitin-conjugating enzyme E2 L3, Ubiquitin C variant, ... (4 entities in total)
• Functional Keywords: e2 ligase, rbr e3 ligase, ubiquitin, heterotrimer, transferase
• Biological source: Homo sapiens (Human); More
• Cellular location: Cytoplasm : Q9Y4X5; Nucleus : P68036
• Total number of polymer chains: 5
• Total formula weight: 157616.87

Authors

Miller, D.J.,Schulman, B.A. (deposition date: 2016-12-27, release date: 2017-06-14, Last modification date: 2024-03-06)

Primary citation

Dove, K.K.,Olszewski, J.L.,Martino, L.,Duda, D.M.,Wu, X.S.,Miller, D.J.,Reiter, K.H.,Rittinger, K.,Schulman, B.A.,Klevit, R.E.
Structural Studies of HHARI/UbcH7Ub Reveal Unique E2Ub Conformational Restriction by RBR RING1.
Structure, 25:890-900.e5, 2017

PubMed Abstract: 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 Zn-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.

PubMed: 28552575
DOI: 10.1016/j.str.2017.04.013

Experimental method

X-RAY DIFFRACTION (3.24 Å)