PDBsum entry 3zo5

Hydrolase/signaling protein

PDB id: 3zo5

Contents

Protein chains

230 a.a.

81 a.a.

Waters ×45

PDB id:

3zo5

Name:

Hydrolase/signaling protein

Title:

Structure of senp2-loop1 in complex with presumo-2

Structure:

Sentrin-specific protease 2. Chain: a. Fragment: residues 363-589. Synonym: axam2, smt3-specific isopeptidase 2, smt3ip2, sentrin/sumo- specific protease senp2, senp2 protease. Engineered: yes. Mutation: yes. Other_details: insertion of ppppakgg instead of f393 and k394 from the senp2 numbering.

Source:

Homo sapiens. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.15Å R-factor: 0.190 R-free: 0.236

Authors:

K.O.Alegre,D.Reverter

Key ref:

K.O.Alegre and D.Reverter (2014). Structural insights into the SENP6 Loop1 structure in complex with SUMO2. Protein Sci, 23, 433-441. PubMed id: 24424631 DOI: 10.1002/pro.2425

Date:

20-Feb-13 Release date: 29-Jan-14

Protein chain

Q9HC62  (SENP2_HUMAN) -  Sentrin-specific protease 2 from Homo sapiens

Seq: 589 a.a.

Struc: 230 a.a.*

Protein chain

P61956  (SUMO2_HUMAN) -  Small ubiquitin-related modifier 2 from Homo sapiens

Seq: 95 a.a.

Struc: 81 a.a.

* PDB and UniProt seqs differ at 9 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chain A: E.C.3.4.22.- - ?????

DOI no: 10.1002/pro.2425

Protein Sci 23:433-441 (2014)

PubMed id: 24424631

Structural insights into the SENP6 Loop1 structure in complex with SUMO2.

K.O.Alegre, D.Reverter.

ABSTRACT

The SENP proteases regulate the SUMO conjugates in the cell by cleaving SUMO from target proteins. SENP6 and SENP7 are the most divergent members of the SENP/ULP protease family in humans by the presence of insertions in their catalytic domains. Loop1 insertion is determinant for the SUMO2/3 activity and specificity on SENP6 and SENP7. To gain structural insights into the role of Loop1, we have designed a chimeric SENP2 with the insertion of Loop1 into its sequence. The structure of SENP2-Loop1 in complex with SUMO2 was solved at 2.15 Å resolution, and reveals the details of an interface exclusive to SENP6/7 and the formation of unique contacts between both proteins. Interestingly, functional data with SUMO substrates showed an increase of the proteolytic activity in the SENP2-Loop1 chimera for diSUMO2 and polySUMO2 substrates.