1Y8X

Structural basis for recruitment of Ubc12 by an E2-binding domain in NEDD8's E1

Summary for 1Y8X

• Entry DOI: 10.2210/pdb1y8x/pdb
• Descriptor: Ubiquitin-conjugating enzyme E2 M, Ubiquitin-activating enzyme E1C (3 entities in total)
• Functional Keywords: ubiquitin-conjugating enzyme e2 m, ligase
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 2
• Total formula weight: 29342.59

Authors

Huang, D.T.,Paydar, A.,Zhuang, M.,Waddell, M.B.,Holton, J.M.,Schulman, B.A. (deposition date: 2004-12-13, release date: 2005-02-08, Last modification date: 2024-11-06)

Primary citation

Huang, D.T.,Paydar, A.,Zhuang, M.,Waddell, M.B.,Holton, J.M.,Schulman, B.A.
Structural basis for recruitment of Ubc12 by an E2 binding domain in NEDD8's E1.
Mol.Cell, 17:341-350, 2005

PubMed Abstract: E2 conjugating enzymes play a central role in ubiquitin and ubiquitin-like protein (ublp) transfer cascades: the E2 accepts the ublp from the E1 enzyme and then the E2 often interacts with an E3 enzyme to promote ublp transfer to the target. We report here the crystal structure of a complex between the C-terminal domain from NEDD8's heterodimeric E1 (APPBP1-UBA3) and the catalytic core domain of NEDD8's E2 (Ubc12). The structure and associated mutational analyses reveal molecular details of Ubc12 recruitment by NEDD8's E1. Interestingly, the E1's Ubc12 binding domain resembles ubiquitin and recruits Ubc12 in a manner mimicking ubiquitin's interactions with ubiquitin binding domains. Structural comparison with E2-E3 complexes indicates that the E1 and E3 binding sites on Ubc12 may overlap and raises the possibility that crosstalk between E1 and E3 interacting with an E2 could influence the specificity and processivity of ublp transfer.

PubMed: 15694336
DOI: 10.1016/j.molcel.2004.12.020

Experimental method

X-RAY DIFFRACTION (2.4 Å)