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Title: A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases

Abstract

How RING E3 ligases mediate E2-to-substrate ubiquitin-like protein (UBL) transfer remains unknown. Here we address how the RING E3 RBX1 positions NEDD8's E2 (UBC12) and substrate (CUL1). We find that existing structures are incompatible with CUL1 NEDD8ylation and report a new conformation of RBX1 that places UBC12 adjacent to CUL1. We propose RING domain rotation as a general mechanism for UBL transfer for the largest family of E3s.

Authors:
; ; ; ; ; ;  [1];  [2]
  1. Cornell
  2. (
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
OTHERNIHHHMI
OSTI Identifier:
1023664
Resource Type:
Journal Article
Journal Name:
Nat. Struct. Mol. Biol.
Additional Journal Information:
Journal Volume: 18; Journal Issue: 2011
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES; LIGASES; PROTEINS; ROTATION; SUBSTRATES

Citation Formats

Calabrese, Matthew F, Scott, Daniel C, Duda, David M, Grace, Christy R.R., Kurinov, Igor, Kriwacki, Richard W, Schulman, Brenda A, and SJCH). A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases. United States: N. p., 2011. Web. doi:10.1038/nsmb.2086.
Calabrese, Matthew F, Scott, Daniel C, Duda, David M, Grace, Christy R.R., Kurinov, Igor, Kriwacki, Richard W, Schulman, Brenda A, & SJCH). A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases. United States. doi:10.1038/nsmb.2086.
Calabrese, Matthew F, Scott, Daniel C, Duda, David M, Grace, Christy R.R., Kurinov, Igor, Kriwacki, Richard W, Schulman, Brenda A, and SJCH). Tue . "A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases". United States. doi:10.1038/nsmb.2086.
@article{osti_1023664,
title = {A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases},
author = {Calabrese, Matthew F and Scott, Daniel C and Duda, David M and Grace, Christy R.R. and Kurinov, Igor and Kriwacki, Richard W and Schulman, Brenda A and SJCH)},
abstractNote = {How RING E3 ligases mediate E2-to-substrate ubiquitin-like protein (UBL) transfer remains unknown. Here we address how the RING E3 RBX1 positions NEDD8's E2 (UBC12) and substrate (CUL1). We find that existing structures are incompatible with CUL1 NEDD8ylation and report a new conformation of RBX1 that places UBC12 adjacent to CUL1. We propose RING domain rotation as a general mechanism for UBL transfer for the largest family of E3s.},
doi = {10.1038/nsmb.2086},
journal = {Nat. Struct. Mol. Biol.},
number = 2011,
volume = 18,
place = {United States},
year = {2011},
month = {9}
}