3TDI

yeast Cul1WHB-Dcn1P acetylated Ubc12N complex

Summary for 3TDI

• Entry DOI: 10.2210/pdb3tdi/pdb
• Related: 3TDU 3TDZ
• Descriptor: Defective in cullin neddylation protein 1, NEDD8-conjugating enzyme UBC12 (3 entities in total)
• Functional Keywords: e2:e3, ligase-protein binding complex, ligase/protein binding
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Total number of polymer chains: 4
• Total formula weight: 54512.04

Authors

Scott, D.C.,Monda, J.K.,Bennett, E.J.,Harper, J.W.,Schulman, B.A. (deposition date: 2011-08-11, release date: 2011-10-12, Last modification date: 2024-11-20)

Primary citation

Scott, D.C.,Monda, J.K.,Bennett, E.J.,Harper, J.W.,Schulman, B.A.
N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex.
Science, 334:674-678, 2011

PubMed Abstract: Although many eukaryotic proteins are amino (N)-terminally acetylated, structural mechanisms by which N-terminal acetylation mediates protein interactions are largely unknown. Here, we found that N-terminal acetylation of the E2 enzyme, Ubc12, dictates distinctive E3-dependent ligation of the ubiquitin-like protein Nedd8 to Cul1. Structural, biochemical, biophysical, and genetic analyses revealed how complete burial of Ubc12's N-acetyl-methionine in a hydrophobic pocket in the E3, Dcn1, promotes cullin neddylation. The results suggest that the N-terminal acetyl both directs Ubc12's interactions with Dcn1 and prevents repulsion of a charged N terminus. Our data provide a link between acetylation and ubiquitin-like protein conjugation and define a mechanism for N-terminal acetylation-dependent recognition.

PubMed: 21940857
DOI: 10.1126/science.1209307

Experimental method

X-RAY DIFFRACTION (2.3 Å)