c-di-AMP recognition by Staphylococcus aureus PstA

FEBS Lett. 2015 Jan 2;589(1):45-51. doi: 10.1016/j.febslet.2014.11.022. Epub 2014 Nov 28.

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.

Keywords: Bacterial signal transduction; Crystal structure; Cyclic-di-AMP; Ferredoxin-like fold; P(II)-related protein.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ATP-Binding Cassette Transporters / chemistry*
  • ATP-Binding Cassette Transporters / genetics
  • ATP-Binding Cassette Transporters / metabolism
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Cell Wall / chemistry
  • Cell Wall / genetics
  • Cell Wall / metabolism
  • Crystallography, X-Ray
  • Dinucleoside Phosphates / chemistry*
  • Dinucleoside Phosphates / genetics
  • Dinucleoside Phosphates / metabolism
  • Models, Molecular
  • Potassium / chemistry
  • Protein Folding*
  • Staphylococcus aureus / chemistry*
  • Staphylococcus aureus / genetics
  • Staphylococcus aureus / metabolism
  • Structural Homology, Protein

Substances

  • ATP-Binding Cassette Transporters
  • Bacterial Proteins
  • Dinucleoside Phosphates
  • cyclic diadenosine phosphate
  • phosphate-specific transport protein A, bacteria
  • Potassium