Structural and functional characterisation of the entry point to pyocyanin biosynthesis in Pseudomonas aeruginosa defines a new 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase subclass

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dc.contributor.authorSterritt, Oliver W.
dc.contributor.authorLang, Eric J. M.
dc.contributor.authorKessans, Sarah A.
dc.contributor.authorRyan, Timothy M.
dc.contributor.authorDemeler, Borries
dc.contributor.authorJameson, Geoffrey B.
dc.contributor.authorParker, Emily J.
dc.date.accessioned2021-09-16T16:16:11Z
dc.date.available2021-09-16T16:16:11Z
dc.date.issued2018
dc.descriptionOpen access article. Creative Commons Attribution 4.0 International license (CC BY 4.0) appliesen_US
dc.description.abstractIn Pseudomonas aeruginosa ( Pae ), the shikimate pathway end product, chorismate, serves as the last common precursor for the biosynthesis of both primary aromatic metabolites, including phenylalanine, tyrosine and tryptophan, and secondary aromatic metabolites, including phenazine-1-carboxylic acid (PCA) and pyocyanin (PYO). The enzyme 3-deoxy- d - arabino -heptulosonate 7-phosphate synthase (DAH7PS) catalyses the first committed step of the shikimate pathway, en route to chorismate. P. aeruginosa expresses multiple, distinct DAH7PSs that are associated with either primary or secondary aromatic compound biosynthesis. Here we report the structure of a type II DAH7PS, encoded by phzC as part of the duplicated phenazine biosynthetic cluster, from P. aeruginosa (PAO1) revealing for the first time the structure of a type II DAH7PS involved in secondary metabolism. The omission of the structural elements α 2a and α 2b , relative to other characterised type II DAH7PSs, leads to the formation of an alternative, dimeric, solution-state structure for this type II DAH7PS with an oligomeric interface that has not previously been characterised and that does not facilitate the formation of aromatic amino acid allosteric binding sites. The sequence similarity and, in particular, the common N-terminal extension suggest a common origin for the type II DAH7PSs from P. aeruginosa. The results described in the present study support an expanded classification of the type II DAH7PSs as type II A and type II B based on sequence characteristics, structure and function of the resultant proteins, and on defined physiological roles within primary or secondary metabolism.en_US
dc.description.peer-reviewYesen_US
dc.identifier.citationSterritt, O. W., Lang, E. J. M., Kessans, S. A., Ryan, T. M., Demeler, B., Jameson, G. B., & Parker, E. J. (2018). Structural and functional characterisation of the entry point to pyocyanin biosynthesis in Pseudomonas aeruginosa defines a new 3-deoxy-d-arabino-arabino-heptulosonate 7-phosphate synthase subclass. Bioscience Reports, 38(5), Article BSR20181605. https://doi.org/10.1042/BSR20181605en_US
dc.identifier.urihttps://hdl.handle.net/10133/6024
dc.language.isoen_USen_US
dc.publisherPortland Pressen_US
dc.publisher.departmentDepartment of Chemistry and Biochemistryen_US
dc.publisher.facultyArts and Scienceen_US
dc.publisher.institutionUniversity of Canterburyen_US
dc.publisher.institutionUniversity of Aucklanden_US
dc.publisher.institutionAustralian Synchrotron/ANSTOen_US
dc.publisher.institutionUniversity of Lethbridgeen_US
dc.publisher.institutionMassey Universityen_US
dc.publisher.institutionVictoria University of Wellingtonen_US
dc.publisher.urlhttps://doi.org/10.1042/BSR20181605en_US
dc.subjectAromatic amino aciden_US
dc.subjectDAHP synthaseen_US
dc.subjectPyocyaninen_US
dc.subjectShikimateen_US
dc.titleStructural and functional characterisation of the entry point to pyocyanin biosynthesis in Pseudomonas aeruginosa defines a new 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase subclassen_US
dc.typeArticleen_US
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