PDBsum entry 2vrn

Hydrolase

PDB id: 2vrn

Contents

Protein chains

185 a.a. *

Metals

_MG

Waters ×172

* Residue conservation analysis

PDB id:

2vrn

Name:

Hydrolase

Title:

The structure of the stress response protein dr1199 from deinococcus radiodurans: a member of the dj-1 superfamily

Structure:

Protease i. Chain: a, b. Synonym: dr1199. Engineered: yes. Other_details: cysteine 115 modified to cysteine sulfenic acid (cso)

Source:

Deinococcus radiodurans. Organism_taxid: 243230. Strain: r1. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008

Resolution:

2.15Å R-factor: 0.203 R-free: 0.261

Authors:

E.Fioravanti,M.A.Dura,D.Lascoux,E.Micossi,S.Mcsweeney

Key ref:

E.Fioravanti et al. (2008). Structure of the stress response protein DR1199 from Deinococcus radiodurans: a member of the DJ-1 superfamily. Biochemistry, 47, 11581-11589. PubMed id: 18850720

Date:

09-Apr-08 Release date: 28-Oct-08

Protein chains

Q9RV31  (Q9RV31_DEIRA) -  Protease I from Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)

Seq: 190 a.a.

Struc: 185 a.a.*

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

Biochemistry 47:11581-11589 (2008)

PubMed id: 18850720

Structure of the stress response protein DR1199 from Deinococcus radiodurans: a member of the DJ-1 superfamily.

E.Fioravanti, M.A.Durá, D.Lascoux, E.Micossi, B.Franzetti, S.McSweeney.

ABSTRACT

The expression level of protein DR1199 is observed to increase considerably in the radio-resistant bacterium Deinococcus radiodurans following irradiation. This protein belongs to the DJ-1 superfamily, which includes proteins with diverse functions, such as the archaeal proteases PhpI and PfpI, the bacterial chaperone Hsp31 and hyperosmotic stress protein YhbO, and the human Parkinson's disease-related protein DJ-1. All members of the superfamily are oligomeric, and the oligomerization interface varies from protein to protein. Although for many of these proteins, their function remains obscure, most of them are involved in cellular protection against environmental stresses. We have determined the structure of DR1199 to a resolution of 2.15 A, and we have tested its function and studied its role in the response to irradiation and more generally to oxidative stress in D. radiodurans. The protein is a dimer displaying an oligomerization interface similar to that observed for the YhbO and PhpI proteins. The cysteine in the catalytic triad (Cys 115) is oxidized in our structure, similar to modifications seen in the corresponding cysteine of the DJ-1 protein. The oxidation occurs spontaneously in DR1199 crystals. In solution, no proteolytic or chaperone activity was detected. On the basis of our results, we suggest that DR1199 might work as a general stress protein involved in the detoxification of the cell from oxygen reactive species, rather than as a peptidase in D. radiodurans.