PDBsum entry 1euv

Hydrolase

PDB id: 1euv

Contents

Protein chains

221 a.a. *

79 a.a. *

Waters ×432

* Residue conservation analysis

PDB id:

1euv

Name:

Hydrolase

Title:

X-ray structure of thE C-terminal ulp1 protease domain in complex with smt3, the yeast ortholog of sumo.

Structure:

Ulp1 protease. Chain: a. Fragment: c-terminal protease domain. Engineered: yes. Ubitqutin-like protein smt3. Chain: b. Fragment: smt3 residues 13-98. Engineered: yes

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Tetramer (from PQS)

Resolution:

1.60Å R-factor: 0.193 R-free: 0.251

Authors:

E.Mossessova,C.D.Lima

Key ref:

E.Mossessova and C.D.Lima (2000). 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. PubMed id: 10882122 DOI: 10.1016/S1097-2765(00)80326-3

Date:

17-Apr-00 Release date: 07-Jun-00

Protein chain

Q02724  (ULP1_YEAST) -  Ubiquitin-like-specific protease 1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 621 a.a.

Struc: 221 a.a.*

Protein chain

Q12306  (SMT3_YEAST) -  Ubiquitin-like protein SMT3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 101 a.a.

Struc: 79 a.a.

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chain A: E.C.3.4.22.68 - Ulp1 peptidase.

DOI no: 10.1016/S1097-2765(00)80326-3

Mol Cell 5:865-876 (2000)

PubMed id: 10882122

Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast.

E.Mossessova, C.D.Lima.

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.

Selected figure(s)

Figure 3.
Figure 3. Structure of the Ulp1-Smt3 ComplexUlp1 is colored blue; Smt3 is colored red.(A) View looking into a side of the complex.(B) A perpendicular view of the complex looking onto the active site. β strands are numbered; α helices are lettered. The C-terminal Smt3 Gly-Gly motif is located above Ulp1 helix F.(C) Stereo representation of the Ulp1-Smt3 complex in an orientation approximately 45° from (A) or (B). Cα positions are numbered every ten residues with Smt3 denoted by a thicker line. Graphics prepared using SETOR unless otherwise noted ([9]).

Figure 5.
Figure 5. Ulp1 Motifs and the Smt3 InterfaceThe Ulp1 polypeptide backbone is depicted in ribbon representation, while the Smt3 peptide is depicted in stick representation. Ulp1 color-coded motifs as in Figure 1. (A) Ulp1 motif 1 (pink); (B) motif 2 (blue); (C) motif 3 (red); and (D) motif 4 (green). Views approximate a close-up for each motif as it appears in Figure 4B. Hydrogen bonds are denoted by black spheres. Waters are depicted by red spheres. Amino acid residues discussed in the text are numbered.

The above figures are reprinted by permission from Cell Press: Mol Cell (2000, 5, 865-876) copyright 2000.

Figures were selected by an automated process.