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The hypothetical periplasmic protein PA1624 from Pseudomonas aeruginosa folds into a unique two-domain structure.

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.

SUBMITTER: Feiler CG

PROVIDER: S-EPMC7716261 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature

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The hypothetical periplasmic protein PA1624 from Pseudomonas aeruginosa folds into a unique two-domain structure.

Feiler Christian G CG Weiss Manfred S MS Blankenfeldt Wulf W

Acta crystallographica. Section F, Structural biology communications 20201130 Pt 12

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 ...[more]

PMID: 33263573

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