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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.

Abstract : 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.
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Allison Williams, Frédéric Veyrier, Mathilde Bonis, Yann Michaud, Bertrand Raynal, et al.. 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.. Acta Crystallographica Section D: Biological Crystallography, International Union of Crystallography, 2014, 70 (10), pp.2631-2639. ⟨10.1107/S1399004714016770⟩. ⟨pasteur-02072472⟩

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