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4WK3

Structure of Staphyloccus aureus PstA

Summary for 4WK3
Entry DOI10.2210/pdb4wk3/pdb
Related4wk1
DescriptorPstA, CHLORIDE ION (3 entities in total)
Functional Keywordspii, signaling protein
Biological sourceStaphylococcus aureus subsp. aureus COL
Total number of polymer chains1
Total formula weight14053.21
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 citationMuller, M.,Hopfner, K.,Witte, G.
c-di-AMP recognition by Staphylococcus aureus PstA.
Febs Lett., 589:45-51, 2015
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.6 Å)
Structure validation

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