3JYB

Crystal Structure of the RetS periplasmic domain

Summary for 3JYB

• Entry DOI: 10.2210/pdb3jyb/pdb
• Descriptor: Sensor protein (2 entities in total)
• Functional Keywords: beta barrel, carbohydrate binding domain, signaling kinase, two component system, rets, kinase, phosphoprotein, transferase
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 2
• Total formula weight: 34053.89

Authors

Jing, X.,Schubot, F.D.,Robinson, H. (deposition date: 2009-09-21, release date: 2010-02-16, Last modification date: 2024-11-20)

Primary citation

Jing, X.,Jaw, J.,Robinson, H.H.,Schubot, F.D.
Crystal structure and oligomeric state of the RetS signaling kinase sensory domain.
Proteins, 78:1631-1640, 2010

PubMed Abstract: The opportunistic pathogen Pseudomonas aeruginosa may cause both acute and chronic-persistent infections in predisposed individuals. Acute infections require the presence of a functional type III secretion system (T3SS), whereas chronic P. aeruginosa infections are characterized by the formation of drug-resistant biofilms. The T3SS and biofilm formation are reciprocally regulated by the signaling kinases LadS, RetS, and GacS. RetS downregulates biofilm formation and upregulates expression of the T3SS through a unique mechanism. RetS forms a heterodimeric complex with GacS and thus prevents GacS autophosphorylation and downstream signaling. The signals that regulate RetS are not known but RetS possesses a distinctive periplasmic sensor domain that is believed to serve as receptor for the regulatory ligand. We have determined the crystal structure of the RetS sensory domain at 2.0 A resolution. The structure closely resembles those of carbohydrate binding modules of other proteins, suggesting that the elusive ligands are likely carbohydrate moieties. In addition to the conserved beta-sandwich structure, the sensory domain features two alpha helices which create a unique surface topology. Protein-protein crosslinking and fluorescence energy transfer experiments also revealed that the sensory domain dimerizes with a dissociation constant of K(d) = 580 +/- 50 nM, a result with interesting implications for our understanding of the underlying signaling mechanism.

PubMed: 20112417
DOI: 10.1002/prot.22679

Experimental method

X-RAY DIFFRACTION (2.04 Å)