2PZH
YbgC thioesterase (Hp0496) from Helicobacter pylori
Summary for 2PZH
| Entry DOI | 10.2210/pdb2pzh/pdb |
| Related | 1LO7 1S5U |
| Descriptor | Hypothetical protein HP_0496 (2 entities in total) |
| Functional Keywords | lipid, acyl-coa, bacterial membrane, tol-pal system, thioesterase, hot-dog fold, hydrolase |
| Biological source | Helicobacter pylori |
| Total number of polymer chains | 4 |
| Total formula weight | 63417.41 |
| Authors | Angelini, A.,Cendron, L.,Goncalves, S.,Zanotti, G.,Terradot, L. (deposition date: 2007-05-18, release date: 2008-04-08, Last modification date: 2023-08-30) |
| Primary citation | Angelini, A.,Cendron, L.,Goncalves, S.,Zanotti, G.,Terradot, L. Structural and enzymatic characterization of HP0496, a YbgC thioesterase from Helicobacter pylori. Proteins, 72:1212-1221, 2008 Cited by PubMed Abstract: YbgC proteins are bacterial acyl-CoA thioesterases associated with the Tol-Pal system. This system is important for cell envelope integrity and is part of the cell division machinery. In E. coli, YbgC associates with the cell membrane and is part of a protein network involved in lipid biogenesis. In the human pathogen Helicobacter pylori, a putative homologue of YbgC, named HP0496, was found to interact with the cytotoxin CagA by two different studies. We have determined its crystal structure and characterized its enzymatic activity. The structure of HP0496 shows that it is a member of the hot-dog family of proteins, with a epsilongamma tetrameric arrangement. Finally, enzymatic assays performed with the purified protein showed that HP0496 is an acyl-CoA thioesterase that favors long-chain substrates. PubMed: 18338382DOI: 10.1002/prot.22014 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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