Structural highlights
Publication Abstract from PubMed
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.
c-di-AMP recognition by Staphylococcus aureus PstA.,Muller M, Hopfner KP, Witte G FEBS Lett. 2015 Jan 2;589(1):45-51. doi: 10.1016/j.febslet.2014.11.022. Epub 2014, Nov 28. PMID:25435171[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Muller M, Hopfner KP, Witte G. 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. PMID:25435171 doi:http://dx.doi.org/10.1016/j.febslet.2014.11.022
