2IY1

SENP1 (mutant) full length SUMO1

Summary for 2IY1

• Entry DOI: 10.2210/pdb2iy1/pdb
• Related: 1A5R 1TGZ 1WYW 1Y8R 1Z5S 2ASQ 2BF8 2CKG 2CKH 2IY0 2IYC 2IYD
• Descriptor: SENTRIN-SPECIFIC PROTEASE 1, SMALL UBIQUITIN-RELATED MODIFIER 1 (3 entities in total)
• Functional Keywords: hydrolase-nuclear protein complex, nuclear protein, ubl conjugation pathway, protease, hydrolase, ubiquitin, thiol protease, protein protein complex, hydrolase/nuclear protein
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Nucleus : Q9P0U3
• Total number of polymer chains: 4
• Total formula weight: 73056.22

Authors

Shen, L.,Dong, C.,Naismith, J.H. (deposition date: 2006-07-11, release date: 2006-08-15, Last modification date: 2024-05-08)

Primary citation

Shen, L.,Tatham, M.H.,Dong, C.,Zagorska, A.,Naismith, J.H.,Hay, R.T.
Sumo Protease Senp1 Induces Isomerization of the Scissile Peptide Bond.
Nat.Struct.Mol.Biol., 13:1069-, 2006

PubMed Abstract: Small ubiquitin-like modifier (SUMO)-specific protease SENP1 processes SUMO-1, SUMO-2 and SUMO-3 to mature forms and deconjugates them from modified proteins. To establish the proteolytic mechanism, we determined structures of catalytically inactive SENP1 bound to SUMO-1-modified RanGAP1 and to unprocessed SUMO-1. In each case, the scissile peptide bond is kinked at a right angle to the C-terminal tail of SUMO-1 and has the cis configuration of the amide nitrogens. SENP1 preferentially processes SUMO-1 over SUMO-2, but binding thermodynamics of full-length SUMO-1 and SUMO-2 to SENP1 and K(m) values for processing are very similar. However, k(cat) values differ by 50-fold. Thus, discrimination between unprocessed SUMO-1 and SUMO-2 by SENP1 is based on a catalytic step rather than substrate binding and is likely to reflect differences in the ability of SENP1 to correctly orientate the scissile bonds in SUMO-1 and SUMO-2.

PubMed: 17099698
DOI: 10.1038/NSMB1172

Experimental method

X-RAY DIFFRACTION (2.46 Å)