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The hypothetical periplasmic protein PA1624 from Pseudomonas aeruginosa folds into a unique two‐domain structure
Author(s) -
Feiler Christian G.,
Weiss Manfred S.,
Blankenfeldt Wulf
Publication year - 2020
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x20014612
Subject(s) - periplasmic space , pseudomonas aeruginosa , opportunistic pathogen , sequence homology , computational biology , human pathogen , homology (biology) , structural similarity , homology modeling , pathogen , protein structure , biology , chemistry , pseudomonas , microbiology and biotechnology , peptide sequence , bacteria , biochemistry , genetics , amino acid , enzyme , escherichia coli , gene
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.