6PBZ
Crystal structure of Escherichia coli GppA
Summary for 6PBZ
| Entry DOI | 10.2210/pdb6pbz/pdb |
| Descriptor | Guanosine-5'-triphosphate,3'-diphosphate pyrophosphatase, CHLORIDE ION (3 entities in total) |
| Functional Keywords | pppgpp, ppgpp, ppx, gppa, hydrolase |
| Biological source | Escherichia coli (strain K12) |
| Total number of polymer chains | 4 |
| Total formula weight | 220007.33 |
| Authors | Song, H.,Shaw, G.X.,Wang, C.,Ji, X. (deposition date: 2019-06-15, release date: 2019-11-20, Last modification date: 2024-03-13) |
| Primary citation | Song, H.,Dharmasena, M.N.,Wang, C.,Shaw, G.X.,Cherry, S.,Tropea, J.E.,Jin, D.J.,Ji, X. Structure and activity of PPX/GppA homologs from Escherichia coli and Helicobacter pylori. Febs J., 287:1865-1885, 2020 Cited by PubMed Abstract: Rapid adaptation to environmental changes is crucial for bacterial survival. Almost all bacteria possess a conserved stringent response system to prompt transcriptional and metabolic responses toward stress. The adaptive process relies on alarmones, guanosine pentaphosphate (pppGpp), and tetraphosphate (ppGpp), to regulate global gene expression. The ppGpp is more potent than pppGpp in the regulatory activity, and pppGpp phosphohydrolase (GppA) plays a key role in (p)ppGpp homeostasis. Sharing a similar domain structure, GppA is indistinguishable from exopolyphosphatase (PPX), which mediates the metabolism of cellular inorganic polyphosphate. Here, our phylogenetic analysis of PPX/GppA homologs in bacteria shows a wide distribution with several distinct subfamilies, and our structural and functional analysis of Escherichia coli GppA and Helicobacter pylori PPX/GppA reveals unique properties of each homolog. These results explain how each homolog possesses its distinct functionality. PubMed: 31679177DOI: 10.1111/febs.15120 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.475 Å) |
Structure validation
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