2Y9M

Pex4p-Pex22p structure

Summary for 2Y9M

• Entry DOI: 10.2210/pdb2y9m/pdb
• Related: 2Y9O 2Y9P
• Descriptor: UBIQUITIN-CONJUGATING ENZYME E2-21 KDA, PEROXISOME ASSEMBLY PROTEIN 22, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: ligase-transport protein complex, ubiquitin conjugating enzyme, e2 complex, peroxisomal protein, alpha-beta-alpha sandwich fold, e2 co-activator, ligase/transport protein
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); More
• Cellular location: Peroxisome: P29340; Peroxisome membrane ; Single- pass membrane protein : P39718
• Total number of polymer chains: 2
• Total formula weight: 34261.31

Authors

Williams, C.,van den Berg, M.,Panjikar, S.,Distel, B.,Wilmanns, M. (deposition date: 2011-02-15, release date: 2011-10-26, Last modification date: 2017-12-13)

Primary citation

Williams, C.,van den Berg, M.,Panjikar, S.,Stanley, W.A.,Distel, B.,Wilmanns, M.
Insights Into Ubiquitin-Conjugating Enzyme/ Co-Activator Interactions from the Structure of the Pex4P:Pex22P Complex.
Embo J., 31:391-, 2011

PubMed Abstract: Ubiquitin-conjugating enzymes (E2s) coordinate distinct types of ubiquitination via specific E3 ligases, to a large number of protein substrates. While many E2 enzymes need only the presence of an E3 ligase for substrate ubiquitination, a number of E2s require additional, non-canonical binding partners to specify their function. Here, we have determined the crystal structure and function of an E2/co-activator assembly, the Pex4p:Pex22p complex. The peroxisome-associated E2 enzyme Pex4p binds the peroxisomal membrane protein Pex22p through a binding site that does not overlap with any other known interaction interface in E2 enzymes. Pex22p association enhances Pex4p's ability to transfer ubiquitin to a substrate in vitro, and Pex22p binding-deficient forms of Pex4p are unable to ubiquitinate the peroxisomal import receptor Pex5p in vivo. Our data demonstrate that the Pex4p:Pex22p assembly, and not Pex4p alone, functions as the E2 enzyme required for Pex5p ubiquitination, establishing a novel mechanism of E2 enzyme regulation.

PubMed: 22085930
DOI: 10.1038/EMBOJ.2011.411

Experimental method

X-RAY DIFFRACTION (2.6 Å)