4WK1

c-di-AMP recognition by Staphylococcus aureus PstA.

(2015) FEBS Lett 589: 45-51

• PubMed: 25435171 Search on PubMed
• DOI: https://doi.org/10.1016/j.febslet.2014.11.022
• Primary Citation of Related Structures:  
  4WK1, 4WK3


• PubMed Abstract: 
  

  Cyclic-di-AMP (c-di-AMP) is a bacterial secondary messenger involved in various processes, including sensing of DNA-integrity, cell wall metabolism and potassium transport. A number of c-di-AMP receptor proteins have recently been identified in Staphylococcus aureus. One of them - PstA - possesses a ferredoxin-like fold and is structurally related to the class of PII signal-transduction proteins. PII proteins are involved in a large number of pathways, most of them associated with nitrogen metabolism. In this study we describe the mode of c-di-AMP binding and subsequent structural changes of S. aureus PstA. An altered architecture in PstA compared to canonical PII proteins results in differences in ligand coordination.

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Organizational Affiliation: 

Ludwig-Maximilians-Universit?t München, Gene Center and Dept. of Biochemistry, Feodor-Lynen-Str. 25, 81377 Munich, Germany.