4WK1

Crystal structure of Staphylococcus aureus PstA in complex with c-di-AMP

Summary for 4WK1

• Entry DOI: 10.2210/pdb4wk1/pdb
• Descriptor: PstA, (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8 ]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: pii, signaling protein
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 1
• Total formula weight: 14716.24

Authors

Mueller, M.,Hopfner, K.-P.,Witte, G. (deposition date: 2014-10-01, release date: 2014-11-26, Last modification date: 2024-01-10)

Primary citation

Muller, M.,Hopfner, K.,Witte, G.
c-di-AMP recognition by Staphylococcus aureus PstA.
Febs Lett., 589:45-51, 2015

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.

PubMed: 25435171
DOI: 10.1016/j.febslet.2014.11.022

Experimental method

X-RAY DIFFRACTION (1.98 Å)