3ZO5

Structure of SENP2-Loop1 in complex with preSUMO-2

Summary for 3ZO5

• Entry DOI: 10.2210/pdb3zo5/pdb
• Descriptor: SENTRIN-SPECIFIC PROTEASE 2, SMALL UBIQUITIN-RELATED MODIFIER 2 (3 entities in total)
• Functional Keywords: hydrolase-signaling protein complex, hydrolase/signaling protein
• Biological source: HOMO SAPIENS; More
• Cellular location: Nucleus, nuclear pore complex: Q9HC62; Nucleus: P61956
• Total number of polymer chains: 2
• Total formula weight: 38119.73

Authors

Alegre, K.O.,Reverter, D. (deposition date: 2013-02-20, release date: 2014-01-29, Last modification date: 2023-12-20)

Primary citation

Alegre, K.O.,Reverter, D.
Structural Insights Into the Senp6 Loop1 Structure in Complex with Sumo2.
Protein Sci., 23:433-, 2014

PubMed Abstract: The SENP proteases regulate the SUMO conjugates in the cell by cleaving SUMO from target proteins. SENP6 and SENP7 are the most divergent members of the SENP/ULP protease family in humans by the presence of insertions in their catalytic domains. Loop1 insertion is determinant for the SUMO2/3 activity and specificity on SENP6 and SENP7. To gain structural insights into the role of Loop1, we have designed a chimeric SENP2 with the insertion of Loop1 into its sequence. The structure of SENP2-Loop1 in complex with SUMO2 was solved at 2.15 Å resolution, and reveals the details of an interface exclusive to SENP6/7 and the formation of unique contacts between both proteins. Interestingly, functional data with SUMO substrates showed an increase of the proteolytic activity in the SENP2-Loop1 chimera for diSUMO2 and polySUMO2 substrates.

PubMed: 24424631
DOI: 10.1002/PRO.2425

Experimental method

X-RAY DIFFRACTION (2.15 Å)