Structural highlights
Publication Abstract from PubMed
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.
The hypothetical periplasmic protein PA1624 from Pseudomonas aeruginosa folds into a unique two-domain structure.,Feiler CG, Weiss MS, Blankenfeldt W Acta Crystallogr F Struct Biol Commun. 2020 Dec 1;76(Pt 12):609-615. doi:, 10.1107/S2053230X20014612. Epub 2020 Nov 30. PMID:33263573[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Feiler CG, Weiss MS, Blankenfeldt W. The hypothetical periplasmic protein PA1624 from Pseudomonas aeruginosa folds into a unique two-domain structure. Acta Crystallogr F Struct Biol Commun. 2020 Dec 1;76(Pt 12):609-615. doi:, 10.1107/S2053230X20014612. Epub 2020 Nov 30. PMID:33263573 doi:http://dx.doi.org/10.1107/S2053230X20014612
