Citation

BibTex format

@article{Campeotto:2015:10.1074/jbc.M114.621789,
author = {Campeotto, I and Zhang, Y and Mladenov, MG and Freemont, PS and Grundling, A},
doi = {10.1074/jbc.M114.621789},
journal = {Journal of Biological Chemistry},
pages = {2888--2901},
title = {Complex Structure and Biochemical Characterization of the Staphylococcus aureus Cyclic Diadenylate Monophosphate (c-di-AMP)-binding Protein PstA, the Founding Member of a New Signal Transduction Protein Family},
url = {http://dx.doi.org/10.1074/jbc.M114.621789},
volume = {290},
year = {2015}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Signaling nucleotides are integral parts of signal transductionsystems allowing bacteria to cope with and rapidly respond tochanges in the environment. The Staphylococcus aureus PII-likesignal transduction protein PstA was recently identified as acyclic diadenylate monophosphate (c-di-AMP)-binding protein.Here, we present the crystal structures of the apo- and c-diAMP-boundPstA protein, which is trimeric in solution as wellas in the crystals. The structures combined with detailed bioinformaticsanalysis revealed that the protein belongs to a newfamily of proteins with a similar core fold but with distinct featuresto classical PII proteins, which usually function in nitrogenmetabolism pathways in bacteria. The complex structurerevealed three identical c-di-AMP-binding sites per trimer witheach binding site at a monomer-monomer interface. Althoughdistinctly different from other cyclic-di-nucleotide-bindingsites, as the half-binding sites are not symmetrical, the complexstructure also highlighted common features for c-di-AMPbindingsites. A comparison between the apo and complexstructures revealed a series of conformational changes thatresult in the ordering of two anti-parallel !-strands that protrudefrom each monomer and allowed us to propose a mechanismon how the PstA protein functions as a signaling transductionprotein.
AU  - Campeotto,I
AU  - Zhang,Y
AU  - Mladenov,MG
AU  - Freemont,PS
AU  - Grundling,A
DO  - 10.1074/jbc.M114.621789
EP  - 2901
PY  - 2015///
SN  - 1083-351X
SP  - 2888
TI  - Complex Structure and Biochemical Characterization of the Staphylococcus aureus Cyclic Diadenylate Monophosphate (c-di-AMP)-binding Protein PstA, the Founding Member of a New Signal Transduction Protein Family
T2  - Journal of Biological Chemistry
UR  - http://dx.doi.org/10.1074/jbc.M114.621789
UR  - http://hdl.handle.net/10044/1/27436
VL  - 290
ER  -
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