Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Two-component signal transduction systems, commonly found in prokaryotes, typically regulate cellular functions in response to environmental conditions through a phosphorylation-dependent process. A new type of response regulator, hp1043 (HP-RR) from Helicobacter pylori, has been recently identified. HP-RR is essential for cell growth and does not require the well known phosphorelay scheme. Unphosphorylated HP-RR binds specifically to its own promoter (P(1043)) and autoregulates the promoter of the tlpB gene (P(tlpB)). We have determined the structure of HP-RR by NMR and x-ray crystallography, revealing a symmetrical dimer with two functional domains. The molecular topology resembles that of the OmpR/PhoB subfamily, however, the symmetrical dimer is stable even in the unphosphorylated state. The dimer interface, formed by three secondary structure elements (alpha4-beta5-alpha5), resembles that of the active, phosphorylated forms of ArcA and PhoB. Several conserved residues of the HP-RR dimeric interface deviate from the OmpR/PhoB subfamily, although there are similar salt bridges and hydrophobic patches within the interface. Our findings reveal how a new type of response regulator protein could function as a cell growth-associated regulator in the absence of post-translational modification.
Structure of an atypical orphan response regulator protein supports a new phosphorylation-independent regulatory mechanism.,Hong E, Lee HM, Ko H, Kim DU, Jeon BY, Jung J, Shin J, Lee SA, Kim Y, Jeon YH, Cheong C, Cho HS, Lee W J Biol Chem. 2007 Jul 13;282(28):20667-75. Epub 2007 May 9. PMID:17491010[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hong E, Lee HM, Ko H, Kim DU, Jeon BY, Jung J, Shin J, Lee SA, Kim Y, Jeon YH, Cheong C, Cho HS, Lee W. Structure of an atypical orphan response regulator protein supports a new phosphorylation-independent regulatory mechanism. J Biol Chem. 2007 Jul 13;282(28):20667-75. Epub 2007 May 9. PMID:17491010 doi:10.1074/jbc.M609104200