2CKH

SENP1-SUMO2 complex

Replaces:  2BZO

Summary for 2CKH

• Entry DOI: 10.2210/pdb2ckh/pdb
• Related: 1WM2 1WM3 1WZ0 2CKG
• Descriptor: SENTRIN-SPECIFIC PROTEASE 1, SMALL UBIQUITIN-RELATED MODIFIER 2 (2 entities in total)
• Functional Keywords: ubl conjugation pathway, nuclear protein, protease co- complex, sumo, protease, hydrolase, thiol protease
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Nucleus : Q9P0U3 P61956
• Total number of polymer chains: 2
• Total formula weight: 35866.27

Authors

Shen, L.N.,Dong, C.,Liu, H.,Hay, R.T.,Naismith, J.H. (deposition date: 2006-04-18, release date: 2006-04-26, Last modification date: 2023-12-13)

Primary citation

Shen, L.N.,Dong, C.,Liu, H.,Naismith, J.H.,Hay, R.T.
The Structure of Senp1-Sumo-2 Complex Suggests a Structural Basis for Discrimination between Sumo Paralogues During Processing.
Biochem.J., 397:279-, 2006

PubMed Abstract: The SUMO (small ubiquitin-like modifier)-specific protease SENP1 (sentrin-specific protease 1) can process the three forms of SUMO to their mature forms and deconjugate SUMO from modified substrates. It has been demonstrated previously that SENP1 processed SUMO-1 more efficiently than SUMO-2, but displayed little difference in its ability to deconjugate the different SUMO paralogues from modified substrates. To determine the basis for this substrate specificity, we have determined the crystal structure of SENP1 in isolation and in a transition-state complex with SUMO-2. The interface between SUMO-2 and SENP1 has a relatively poor complementarity, and most of the recognition is determined by interaction between the conserved C-terminus of SUMO-2 and the cleft in the protease. Although SENP1 is rather similar in structure to the related protease SENP2, these proteases have different SUMO-processing activities. Electrostatic analysis of SENP1 in the region where the C-terminal peptide, removed during maturation, would project indicates that it is the electrostatic complementarity between this region of SENP1 and the C-terminal peptides of the various SUMO paralogues that mediates selectivity.

PubMed: 16553580
DOI: 10.1042/BJ20052030

Experimental method

X-RAY DIFFRACTION (3.2 Å)