c-di-AMP recognition by Staphylococcus aureus PstA

• Published in: FEBS letters Vol. 589; no. 1; pp. 45 - 51
• Main Authors: Müller, Martina, Hopfner, Karl-Peter, Witte, Gregor
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 02-01-2015
• Subjects: ATP-Binding Cassette Transporters - chemistry; ATP-Binding Cassette Transporters - genetics; ATP-Binding Cassette Transporters - metabolism; Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Bacterial signal transduction; Cell Wall - chemistry; Cell Wall - genetics; Cell Wall - metabolism; Crystal structure; Crystallography, X-Ray; Cyclic-di-AMP; Dinucleoside Phosphates - chemistry; Dinucleoside Phosphates - genetics; Dinucleoside Phosphates - metabolism; Ferredoxin-like fold; Models, Molecular; PII-related protein; Potassium - chemistry; Protein Folding; Staphylococcus aureus; Staphylococcus aureus - chemistry; Staphylococcus aureus - genetics; Staphylococcus aureus - metabolism; Structural Homology, Protein; PII-related protein; Ferredoxin-like fold; Bacterial signal transduction; Cyclic-di-AMP; Crystal structure; P(II)-related protein
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/j.febslet.2014.11.022

•We solved the crystal structure of S. aureus PstA with and without c-di-AMP.•PstA has a ferredoxin-like fold similar to PII-proteins.•PstA has a different loop organization compared to canonical PII-proteins.•PstA shows high affinity binding of c-di-AMP.•c-di-AMP binding leads to loop reorganization in PstA.
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.