5OK8
Crystal structure of protein Lpp20 (HP1456) from Helicobacter pylori
Summary for 5OK8
| Entry DOI | 10.2210/pdb5ok8/pdb |
| Descriptor | LPP20 lipoprotein, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | virulence factor; helicobacter pylori; lipoprotein, unknown function |
| Biological source | Helicobacter pylori (strain J99 / ATCC 700824) |
| Cellular location | Cell outer membrane ; Lipid- anchor : P0A0V1 |
| Total number of polymer chains | 4 |
| Total formula weight | 76838.90 |
| Authors | Zanotti, G.,Mishra, N.,Valesse, F. (deposition date: 2017-07-25, release date: 2017-12-06, Last modification date: 2024-05-08) |
| Primary citation | Vallese, F.,Mishra, N.M.,Pagliari, M.,Berto, P.,Codolo, G.,de Bernard, M.,Zanotti, G. Helicobacter pylori antigenic Lpp20 is a structural homologue of Tip alpha and promotes epithelial-mesenchymal transition. Biochim. Biophys. Acta, 1861:3263-3271, 2017 Cited by PubMed Abstract: Helicobacter pylori is a bacterium that affects about 50% of the world population and, despite being often asymptomatic, it is responsible of several gastric diseases, from gastritis to gastric cancer. The protein Lpp20 (HP1456) plays an important role in bacterium survival and host colonization, but the possibility that it might be involved in the etiology of H. pylori-related disorders is an unexplored issue. Lpp20 is a lipoprotein bound to the external membrane of the bacterium, but it is also secreted inside vesicles along with other two proteins of the same operon, i.e. HP1454 and HP1457. PubMed: 28947343DOI: 10.1016/j.bbagen.2017.09.017 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.874 Å) |
Structure validation
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