Structural characterization of aspartate-semialdehyde dehydrogenase from Pseudomonas aeruginosa and Neisseria gonorrhoeae

S. L. Teakel, J. W. Fairman, M. M. Muruthi, J. Abendroth, D. M. Dranow, D. D. Lorimer, P. J. Myler, T. E. Edwards, J. K. Forwood

Research output: Contribution to journalArticlepeer-review

Abstract

Gonorrhoea infection rates and the risk of infection from opportunistic pathogens including P. aeruginosa have both risen globally, in part due to increasing broad-spectrum antibiotic resistance. Development of new antimicrobial drugs is necessary and urgent to counter infections from drug resistant bacteria. Aspartate-semialdehyde dehydrogenase (ASADH) is a key enzyme in the aspartate biosynthetic pathway, which is critical for amino acid and metabolite biosynthesis in most microorganisms including important human pathogens. Here we present the first structures of two ASADH proteins from N. gonorrhoeae and P. aeruginosa solved by X-ray crystallography. These high-resolution structures present an ideal platform for in silico drug design, offering potential targets for antimicrobial drug development as emerging multidrug resistant strains of bacteria become more prevalent.

Original languageEnglish
Pages (from-to)14010
Number of pages1
JournalScientific Reports
Volume12
Issue number1
DOIs
Publication statusPublished - 17 Aug 2022

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