4JJQ

Crystal structure of usp7-ntd with an e2 enzyme

Summary for 4JJQ

• Entry DOI: 10.2210/pdb4jjq/pdb
• Descriptor: Ubiquitin carboxyl-terminal hydrolase 7, Ubiquitin-conjugating enzyme E2 E1 (3 entities in total)
• Functional Keywords: deubiquitinating enzyme, hydrolase, traf domain, ube2e1
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus : Q93009 P51965
• Total number of polymer chains: 2
• Total formula weight: 19457.43

Authors

Saridakis, V. (deposition date: 2013-03-08, release date: 2013-05-01, Last modification date: 2023-09-20)

Primary citation

Sarkari, F.,Wheaton, K.,La Delfa, A.,Mohamed, M.,Shaikh, F.,Khatun, R.,Arrowsmith, C.H.,Frappier, L.,Saridakis, V.,Sheng, Y.
Ubiquitin-specific protease 7 is a regulator of ubiquitin-conjugating enzyme UbE2E1.
J. Biol. Chem., 288:16975-16985, 2013

PubMed Abstract: Ubiquitin-specific protease 7 (USP7) is a deubiquitinating enzyme found in all eukaryotes that catalyzes the removal of ubiquitin from specific target proteins. Here, we report that UbE2E1, an E2 ubiquitin conjugation enzyme with a unique N-terminal extension, is a novel USP7-interacting protein. USP7 forms a complex with UbE2E1 in vitro and in vivo through the ASTS USP7 binding motif within its N-terminal extension in an identical manner with other known USP7 binding proteins. We show that USP7 attenuates UbE2E1-mediated ubiquitination, an effect that requires the N-terminal ASTS sequence of UbE2E1 as well as the catalytic activity of USP7. Additionally, USP7 is critical in maintaining the steady state levels of UbE2E1 in cells. This study reveals a new cellular mechanism that couples the opposing activities of the ubiquitination machinery and a deubiquitinating enzyme to maintain and modulate the dynamic balance of the ubiquitin-proteasome system.

PubMed: 23603909
DOI: 10.1074/jbc.M113.469262

Experimental method

X-RAY DIFFRACTION (1.95 Å)