PDBsum entry 2q0j

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protein ligands metals Protein-protein interface(s) links
Metal binding protein PDB id
Protein chains
310 a.a. *
BEZ ×2
_FE ×4
Waters ×376
* Residue conservation analysis
PDB id:
Name: Metal binding protein
Title: Structure of pseudomonas quinolone signal response protein pqse
Structure: Quinolone signal response protein. Chain: a, b. Engineered: yes
Source: Pseudomonas aeruginosa. Organism_taxid: 287. Strain: pao1. Gene: pqse. Expressed in: escherichia coli. Expression_system_taxid: 562.
2.10Å     R-factor:   0.154     R-free:   0.211
Authors: S.Yu,V.Jensen,I.Feldmann,S.Haussler,W.Blankenfeldt
Key ref: S.Yu et al. (2009). Structure elucidation and preliminary assessment of hydrolase activity of PqsE, the Pseudomonas quinolone signal (PQS) response protein. Biochemistry, 48, 10298-10307. PubMed id: 19788310
22-May-07     Release date:   03-Jun-08    
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Protein chains
Pfam   ArchSchema ?
P20581  (Y1000_PSEAE) -  Uncharacterized protein PA1000
301 a.a.
310 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     secondary metabolite biosynthetic process   1 term 


Biochemistry 48:10298-10307 (2009)
PubMed id: 19788310  
Structure elucidation and preliminary assessment of hydrolase activity of PqsE, the Pseudomonas quinolone signal (PQS) response protein.
S.Yu, V.Jensen, J.Seeliger, I.Feldmann, S.Weber, E.Schleicher, S.Häussler, W.Blankenfeldt.
In bacteria, the transcription of virulence genes is usually controlled by a cell density-dependent process known as "quorum sensing" (QS). QS relies on small diffusible signaling molecules that cross the bacterial cell wall and activate target transcription factors after a threshold concentration has been reached. Besides two hierarchical QS circuits based on N-acylhomoserine lactones, the human opportunistic pathogen Pseudomonas aeruginosa integrates a signaling system that depends on 2-heptyl-3-hydroxy-4-quinolone, termed "Pseudomonas quinolone signal" (PQS). PQS is produced from genes encoded in the pqs operon, which in addition to the biosynthetic enzymes PqsA-D contains a fifth gene, pqsE, that is not required for production of PQS but whose disruption leads to loss of signal transduction in several but not all pqs operon-dependent processes. PqsE was hence termed "PQS response protein", but its exact mechanism of action is unknown. We have determined the crystal structure of recombinant PqsE and show that it possesses a metallo-beta-lactamase fold with an Fe(II)Fe(III) center in the active site. A copurified ligand was assigned as benzoate and may indicate that PqsE exerts its regulatory effect by converting a chorismate-derived molecule. Further, PqsE was found to slowly hydrolyze phosphodiesters including single- and double-stranded DNA as well as mRNA and also the thioester S-(4-nitrobenzoyl)mercaptoethane. Higher activity was observed after incubation with Co(2+) and, to lesser entent, Mn(2+), suggesting that the Fe(II)Fe(III) center of recombinant PqsE may be an artifact of heterologous expression. A crystal complex of the E182A mutant with bis-pNPP was obtained and suggests a catalytic mechanism for hydrolysis.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20738404 S.Heeb, M.P.Fletcher, S.R.Chhabra, S.P.Diggle, P.Williams, and M.Cámara (2011).
Quinolones: from antibiotics to autoinducers.
  FEMS Microbiol Rev, 35, 247-274.  
20544975 A.Shimada, H.Ishikawa, N.Nakagawa, S.Kuramitsu, and R.Masui (2010).
The first crystal structure of an archaeal metallo-beta-lactamase superfamily protein; ST1585 from Sulfolobus tokodaii.
  Proteins, 78, 2399-2402.
PDB code: 3adr
  20406282 G.Rampioni, C.Pustelny, M.P.Fletcher, V.J.Wright, M.Bruce, K.P.Rumbaugh, S.Heeb, M.Cámara, and P.Williams (2010).
Transcriptomic analysis reveals a global alkyl-quinolone-independent regulatory role for PqsE in facilitating the environmental adaptation of Pseudomonas aeruginosa to plant and animal hosts.
  Environ Microbiol, 12, 1659-1673.  
20300606 R.Hazan, J.He, G.Xiao, V.Dekimpe, Y.Apidianakis, B.Lesic, C.Astrakas, E.Déziel, F.Lépine, and L.G.Rahme (2010).
Homeostatic interplay between bacterial cell-cell signaling and iron in virulence.
  PLoS Pathog, 6, e1000810.  
20525783 R.Norel, D.Petrey, and B.Honig (2010).
PUDGE: a flexible, interactive server for protein structure prediction.
  Nucleic Acids Res, 38, W550-W554.  
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