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Publication Abstract from PubMed

CpxP is a novel bacterial periplasmic protein with no homologues of known function. In Gram-negative enteric bacteria, CpxP is thought to interact with the two-component sensor kinase, CpxA, to inhibit induction of the Cpx envelope stress response in the absence of protein misfolding. CpxP has also been shown to facilitate DegP-mediated proteolysis of misfolded proteins. Six mutations that negate the ability of CpxP to function as a signaling protein are localized in or near two conserved LTXXQ motifs that define a class of proteins with similarity to CpxP, Pfam PF07813. To gain insight into how these mutations might affect CpxP signaling and/or proteolytic adaptor functions, the crystal structure of CpxP from Escherichia coli was determined to 2.85 A resolution. The structure revealed an antiparallel dimer of intertwined alpha-helices with a highly basic concave surface. Each protomer consists of a long, hooked and bent hairpin fold with the conserved LTXXQ motifs forming two diverging turns at one end. Biochemical studies demonstrated that CpxP maintains a dimeric state, but may undergo a slight structural adjustment in response to the inducing cue, alkaline pH. Three of the six previously characterized cpxP loss-of-function mutations, M59T, Q55P, and Q128H, likely result from a destabilization of the protein fold, whereas the R60Q, D61E, and D61V mutations may alter intermolecular interactions.

Structure of the periplasmic stress response protein CpxP.,Thede GL, Arthur DC, Edwards RA, Buelow DR, Wong JL, Raivio TL, Glover JN J Bacteriol. 2011 Feb 11. PMID:21317318^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.