2hkp

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2hkp, resolution 2.100Å

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SUMO protease Ulp1 with the catalytic cysteine oxidized to a sulfenic acid

Overview

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.

About this Structure

2HKP is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast., Mossessova E, Lima CD, Mol Cell. 2000 May;5(5):865-76. PMID:10882122

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