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dc.contributor.author Sterritt, Oliver W.
dc.contributor.author Lang, Eric J. M.
dc.contributor.author Kessans, Sarah A.
dc.contributor.author Ryan, Timothy M.
dc.contributor.author Demeler, Borries
dc.contributor.author Jameson, Geoffrey B.
dc.contributor.author Parker, Emily J.
dc.date.accessioned 2021-09-16T16:16:11Z
dc.date.available 2021-09-16T16:16:11Z
dc.date.issued 2018
dc.identifier.citation Sterritt, 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/BSR20181605 en_US
dc.identifier.uri https://hdl.handle.net/10133/6024
dc.description Open access article. Creative Commons Attribution 4.0 International license (CC BY 4.0) applies en_US
dc.description.abstract In 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.language.iso en_US en_US
dc.publisher Portland Press en_US
dc.subject Aromatic amino acid en_US
dc.subject DAHP synthase en_US
dc.subject Pyocyanin en_US
dc.subject Shikimate en_US
dc.title 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 en_US
dc.type Article en_US
dc.publisher.faculty Arts and Science en_US
dc.publisher.department Department of Chemistry and Biochemistry en_US
dc.description.peer-review Yes en_US
dc.publisher.institution University of Canterbury en_US
dc.publisher.institution University of Auckland en_US
dc.publisher.institution Australian Synchrotron/ANSTO en_US
dc.publisher.institution University of Lethbridge en_US
dc.publisher.institution Massey University en_US
dc.publisher.institution Victoria University of Wellington en_US
dc.publisher.url https://doi.org/10.1042/BSR20181605 en_US


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