1EUV

X-RAY STRUCTURE OF THE C-TERMINAL ULP1 PROTEASE DOMAIN IN COMPLEX WITH SMT3, THE YEAST ORTHOLOG OF SUMO.

Summary for 1EUV

• Entry DOI: 10.2210/pdb1euv/pdb
• Descriptor: ULP1 PROTEASE, UBITQUTIN-LIKE PROTEIN SMT3 (3 entities in total)
• Functional Keywords: sumo hydrolase, ubiquitin-like protease 1, smt3 hydrolase desumoylating enzyme, cysteine protease, sumo processing enzyme, smt3 processing enzyme, nabh4, thiohemiacetal, covalent protease adduct, hydrolase
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Total number of polymer chains: 2
• Total formula weight: 35611.58

Authors

Mossessova, E.,Lima, C.D. (deposition date: 2000-04-17, release date: 2000-06-07, Last modification date: 2024-11-13)

Primary citation

Mossessova, E.,Lima, C.D.
Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast.
Mol.Cell, 5:865-876, 2000

PubMed Abstract: Modification of cellular proteins by the ubiquitin-like protein SUMO is essential for nuclear processes and cell cycle progression in yeast. The Ulp1 protease catalyzes two essential functions in the SUMO pathway: (1) processing of full-length SUMO to its mature form and (2) deconjugation of SUMO from targeted proteins. Selective reduction of the proteolytic reaction produced a covalent thiohemiacetal transition state complex between a Ulp1 C-terminal fragment and its cellular substrate Smt3, the yeast SUMO homolog. The Ulp1-Smt3 crystal structure and functional testing of elements within the conserved interface elucidate determinants of SUMO recognition, processing, and deconjugation. Genetic analysis guided by the structure further reveals a regulatory element N-terminal to the proteolytic domain that is required for cell growth in yeast.

PubMed: 10882122
DOI: 10.1016/S1097-2765(00)80326-3

Experimental method

X-RAY DIFFRACTION (1.6 Å)