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© Ahmed Haouz
Cristaux d'une protéine de Mycobacterium tuberculosis produits dans le cadre du Grand Programme Horizontal sur la Tuberculose à l'Institut Pasteur. La caractérisation structurale de protéines mycobactériennes aide à une meilleure compréhension de la physiologie et de la pathogénicité des mycobactéries et fournit un point de départ pour la conception de nouveaux agents antibactériens.
Publication : Acta crystallographica. Section D, Biological crystallography

Visualization of a substrate-induced productive conformation of the catalytic triad of the Neisseria meningitidis peptidoglycan O-acetylesterase reveals mechanistic conservation in SGNH esterase family members

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Acta crystallographica. Section D, Biological crystallography - 27 Sep 2014

Williams AH, Veyrier FJ, Bonis M, Michaud Y, Raynal B, Taha MK, White SW, Haouz A, Boneca IG

Link to Pubmed [PMID] – 25286847

Acta Crystallogr. D Biol. Crystallogr. 2014 Oct;70(Pt 10):2631-9

Peptidoglycan O-acetylesterase (Ape1), which is required for host survival in Neisseria sp., belongs to the diverse SGNH hydrolase superfamily, which includes important viral and bacterial virulence factors. Here, multi-domain crystal structures of Ape1 with an SGNH catalytic domain and a newly identified putative peptidoglycan-detection module are reported. Enzyme catalysis was performed in Ape1 crystals and key catalytic intermediates along the SGNH esterase hydrolysis reaction pathway were visualized, revealing a substrate-induced productive conformation of the catalytic triad, a mechanistic detail that has not previously been observed. This substrate-induced productive conformation of the catalytic triad shifts the established dogma on these enzymes, generating valuable insight into the structure-based design of drugs targeting the SGNH esterase superfamily.

https://www.ncbi.nlm.nih.gov/pubmed/25286847