6BMC

The structure of a dimeric type II DAH7PS associated with pyocyanin biosynthesis in Pseudomonas aeruginosa

Summary for 6BMC

• Entry DOI: 10.2210/pdb6bmc/pdb
• Related: 2B7O 5UXM 5UXN 5UXO
• Descriptor: Phospho-2-dehydro-3-deoxyheptonate aldolase, PHOSPHOENOLPYRUVATE, COBALT (II) ION, ... (5 entities in total)
• Functional Keywords: transferase, dah7ps, 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase, shikimate pathway, pyocyanin biosynthesis
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 2
• Total formula weight: 89268.57

Authors

Sterritt, O.W.,Jameson, G.B.,Parker, E.J. (deposition date: 2017-11-14, release date: 2018-10-03, Last modification date: 2023-10-04)

Primary citation

Sterritt, O.W.,Lang, E.J.M.,Kessans, S.A.,Ryan, T.M.,Demeler, B.,Jameson, G.B.,Parker, E.J.
Structural and functional characterisation of the entry point to pyocyanin biosynthesis inPseudomonas aeruginosadefines a new 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase subclass.
Biosci. Rep., 38:-, 2018

PubMed Abstract: In (), 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--heptulosonate 7-phosphate synthase (DAH7PS) catalyses the first committed step of the shikimate pathway, en route to chorismate. 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 as part of the duplicated phenazine biosynthetic cluster, from (PAO1) revealing for the first time the structure of a type II DAH7PS involved in secondary metabolism. The omission of the structural elements α and α, 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 The results described in the present study support an expanded classification of the type II DAH7PSs as type II and type II based on sequence characteristics, structure and function of the resultant proteins, and on defined physiological roles within primary or secondary metabolism.

PubMed: 30242059
DOI: 10.1042/BSR20181605

Experimental method

X-RAY DIFFRACTION (2.7 Å)