title: Structural insights into the SENP6 Loop1 structure in complex with SUMO2.
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.
authors.affiliation: Institut de Biotecnologia i de Biomedicina and Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, 08193, Bellaterra, Spain.
authors.forename: Kamela O
authors.initials: KO
authors.lastname: Alegre
authors.forename: David
authors.initials: D
authors.lastname: Reverter
mesh_terms: D003546:Cysteine Endopeptidases / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D011487:Protein Conformation; D025841:Small Ubiquitin-Related Modifier Proteins / Q000737:chemistry* / Q000378:metabolism
chemical_list: C117909:SUMO2 protein, human; D025841:Small Ubiquitin-Related Modifier Proteins; D003546:Cysteine Endopeptidases; C408873:SENP6 protein, human
keywords: SENP2; SENP6; SENP7; SUMO; polySUMO chain; ubiquitin-like protein