6TD9
X-ray structure of mature PA1624 from Pseudomonas aeruginosa PAO1
Summary for 6TD9
| Entry DOI | 10.2210/pdb6td9/pdb |
| Descriptor | PA1624, 1,2-ETHANEDIOL, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, ... (5 entities in total) |
| Functional Keywords | periplasmic protein, unique fold, unknown function |
| Biological source | Pseudomonas aeruginosa PAO1 |
| Total number of polymer chains | 2 |
| Total formula weight | 55990.68 |
| Authors | Feiler, C.G.,Blankenfeldt, W. (deposition date: 2019-11-08, release date: 2019-12-04, Last modification date: 2024-11-13) |
| Primary citation | Feiler, C.G.,Weiss, M.S.,Blankenfeldt, W. The hypothetical periplasmic protein PA1624 from Pseudomonas aeruginosa folds into a unique two-domain structure. Acta Crystallogr.,Sect.F, 76:609-615, 2020 Cited by PubMed Abstract: The crystal structure of the 268-residue periplasmic protein PA1624 from the opportunistic pathogen Pseudomonas aeruginosa PAO1 was determined to high resolution using the Se-SAD method for initial phasing. The protein was found to be monomeric and the structure consists of two domains, domains 1 and 2, comprising residues 24-184 and 185-268, respectively. The fold of these domains could not be predicted even using state-of-the-art prediction methods, and similarity searches revealed only a very distant homology to known structures, namely to Mog1p/PsbP-like and OmpA-like proteins for the N- and C-terminal domains, respectively. Since PA1624 is only present in an important human pathogen, its unique structure and periplasmic location render it a potential drug target. Consequently, the results presented here may open new avenues for the discovery and design of antibacterial drugs. PubMed: 33263573DOI: 10.1107/S2053230X20014612 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.96 Å) |
Structure validation
Download full validation report
