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An active site water network in the plasminogen activator pla from Yersinia pestis.

Eren E, Murphy M, Goguen J, van den Berg B
Structure 18 809-18 (2010)
Related entries: 2x55, 2x56

Cited: 32 times
EuropePMC logo PMID: 20637417

Abstract

The plasminogen activator Pla from Yersinia pestis is an outer membrane protease (omptin) that is important for the virulence of plague. Here, we present the high-resolution crystal structure of wild-type, enzymatically active Pla at 1.9 A. The structure shows a water molecule located between active site residues D84 and H208, which likely corresponds to the nucleophilic water. A number of other water molecules are present in the active site, linking residues important for enzymatic activity. The R211 sidechain in loop L4 is close to the nucleophilic water and possibly involved in the stabilization of the oxyanion intermediate. Subtle conformational changes of H208 result from the binding of lipopolysaccharide to the outside of the barrel, explaining the unusual dependence of omptins on lipopolysaccharide for activity. The Pla structure suggests a model for the interaction with plasminogen substrate and provides a more detailed understanding of the catalytic mechanism of omptin proteases.

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Reviews citing this publication (7)

  1. Emerging Diversity in Lipid-Protein Interactions. Corradi V, Sejdiu BI, Mesa-Galloso H, Abdizadeh H, Noskov SY, Marrink SJ, Tieleman DP. Chem Rev 119 5775-5848 (2019)
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  4. Production of outer membrane vesicles by the plague pathogen Yersinia pestis. Eddy JL, Gielda LM, Caulfield AJ, Rangel SM, Lathem WW. PLoS One 9 e107002 (2014)
  5. The Xanthomonas Ax21 protein is processed by the general secretory system and is secreted in association with outer membrane vesicles. Bahar O, Pruitt R, Luu DD, Schwessinger B, Daudi A, Liu F, Ruan R, Fontaine-Bodin L, Koebnik R, Ronald P. PeerJ 2 e242 (2014)
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  8. The outer membrane protease PgtE of Salmonella enterica interferes with the alternative complement pathway by cleaving factors B and H. Riva R, Korhonen TK, Meri S. Front Microbiol 6 63 (2015)
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  10. Pathogenicity of Yersinia pestis synthesis of 1-dephosphorylated lipid A. Sun W, Six DA, Reynolds CM, Chung HS, Raetz CR, Curtiss R. Infect Immun 81 1172-1185 (2013)
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  12. Antimicrobial Peptide Conformation as a Structural Determinant of Omptin Protease Specificity. Brannon JR, Thomassin JL, Gruenheid S, Le Moual H. J Bacteriol 197 3583-3591 (2015)
  13. Folding of outer membrane protein A in the anionic biosurfactant rhamnolipid. Andersen KK, Otzen DE. FEBS Lett 588 1955-1960 (2014)
  14. Genomic Insights into a New Citrobacter koseri Strain Revealed Gene Exchanges with the Virulence-Associated Yersinia pestis pPCP1 Plasmid. Armougom F, Bitam I, Croce O, Merhej V, Barassi L, Nguyen TT, La Scola B, Raoult D. Front Microbiol 7 340 (2016)
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