ArticleActa crystallographica. Section D, Biological crystallography2014
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.
Article in Acta crystallographica. Section D, Biological crystallography, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- Article
- The SGNH hydrolase family: a template for carbohydrate diversity.Glycobiology · 2022Review
- CE16 acetylesterases: in silico analysis, catalytic machinery prediction and comparison with related SGNH hydrolases.3 Biotech · 2021Article
- Structural basis for theThe Journal of biological chemistry · 2020Article
- A pair of esterases from a commensal gut bacterium remove acetylations from all positions on complex β-mannans.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Development of a High Throughput Screen for the Identification of Inhibitors of PeptidoglycanAntibiotics (Basel, Switzerland) · 2019Article
- Mechanistic Pathways for Peptidoglycan O-Acetylation and De-O-Acetylation.Frontiers in microbiology · 2018Review
- In vitro characterization of the antivirulence target of Gram-positive pathogens, peptidoglycan O-acetyltransferase A (OatA).PLoS pathogens · 2017Article
- Accumulation of Peptidoglycan O-Acetylation Leads to Altered Cell Wall Biochemistry and Negatively Impacts Pathogenesis Factors of Campylobacter jejuni.The Journal of biological chemistry · 2016Article
- Crystal structure of an acetyl esterase complexed with acetate ion provides insights into the catalytic mechanism.Biochemical and biophysical research communications · 2016Article
- Coronavirus receptor switch explained from the stereochemistry of protein-carbohydrate interactions and a single mutation.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- 9-O-Acetylation of sialic acids is catalysed by CASD1 via a covalent acetyl-enzyme intermediate.Nature communications · 2015Article
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Authors and funding
9 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
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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