4WK3
Structure of Staphyloccus aureus PstA
Summary for 4WK3
| Entry DOI | 10.2210/pdb4wk3/pdb |
| Related | 4wk1 |
| Descriptor | PstA, CHLORIDE ION (3 entities in total) |
| Functional Keywords | pii, signaling protein |
| Biological source | Staphylococcus aureus subsp. aureus COL |
| Total number of polymer chains | 1 |
| Total formula weight | 14053.21 |
| 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 citation | Muller, 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: 25435171DOI: 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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