ArticleMolecular microbiology2016
The crystal structure of the major pneumococcal autolysin LytA in complex with a large peptidoglycan fragment reveals the pivotal role of glycans for lytic activity.
Article in Molecular microbiology, 2016. 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, 19 citations in OpenAlex.
- Streptococcus pneumoniae synchronizes the states of cell wall peptidoglycan acetylation and genome methylation by programmed DNA inversions.PLoS pathogens · 2025Article
- Deep Antimicrobial Activity and Stability Analysis Inform Lysin Sequence-Function Mapping.ACS synthetic biology · 2023Article
- Implications of oral streptococcal bacteriophages in autism spectrum disorder.NPJ biofilms and microbiomes · 2022Article
- THCz: Small molecules with antimicrobial activity that block cell wall lipid intermediates.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- A Choline-Recognizing Monomeric Lysin, ClyJ-3m, Shows Elevated Activity against Streptococcus pneumoniae.Antimicrobial agents and chemotherapy · 2020Article
- Computationally Aided Discovery of LysEFm5 Variants with Improved Catalytic Activity and Stability.Applied and environmental microbiology · 2020Article
- A switch in surface polymer biogenesis triggers growth-phase-dependent and antibiotic-induced bacteriolysis.eLife · 2019Article
- ClyJ Is a Novel Pneumococcal Chimeric Lysin with a Cysteine- and Histidine-Dependent Amidohydrolase/Peptidase Catalytic Domain.Antimicrobial agents and chemotherapy · 2019Article
- Structure and function of the Ts2631 endolysin of Thermus scotoductus phage vB_Tsc2631 with unique N-terminal extension used for peptidoglycan binding.Scientific reports · 2019Article
- A choline binding polypeptide of LytA inhibits the growth of Streptococcus pneumoniae by binding to choline in the cell wall.The Journal of antibiotics · 2018Article
- Peptidoglycan O-acetylation is functionally related to cell wall biosynthesis and cell division in Streptococcus pneumoniae.Molecular microbiology · 2017Article
- Bacterial size matters: Multiple mechanisms controlling septum cleavage and diplococcus formation are critical for the virulence of the opportunistic pathogen Enterococcus faecalis.PLoS pathogens · 2017Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
The pneumococcal autolysin LytA is a key virulence factor involved in several important functions including DNA competence, immune evasion and biofilm formation. Here, we present the 1.05 Å crystal structure of the catalytic domain of LytA in complex with a synthetic cell-wall-based peptidoglycan (PG) ligand that occupies the entire Y-shaped substrate-binding crevice. As many as twenty-one amino-acid residues are engaged in ligand interactions with a majority of these interactions directed towards the glycan strand. All saccharides are intimately bound through hydrogen bond, van der Waals and CH-π interactions. Importantly, the structure of LytA is not altered upon ligand binding, whereas the bound ligand assumes a different conformation compared to the unbound NMR-based solution structure of the same PG-fragment. Mutational study reveals that several non-catalytic glycan-interacting residues, structurally conserved in other amidases from Gram-positive Firmicutes, are pivotal for enzymatic activity. The three-dimensional structure of the LytA/PG complex provides a novel structural basis for ligand restriction by the pneumococcal autolysin, revealing for the first time an importance of the multivalent binding to PG saccharides.
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