LysM, a widely distributed protein motif for binding to (peptido)glycans

By G. Buist, Anton Steen, Jan Kok, Oscar P. Kuipers. Molecular Microbiology, 2008

647 citations recorded by the source corpus.

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

The extracellular biology of the lactobacilli (2010, background): “metabolism, and is suggested to confer general peptidoglycan binding function (Buist et al., 2008).”
A Phage Tail-Derived Element with Wide Distribution among Both Prokaryotic Domains: A Comparative Genomic and Phylogenetic Study (2014, background): “Although the LysM- motif bearing ORF is highly conserved in sequence and position within PLTS clusters, the absence of domains exhibiting hydrolase activity consequently suggests that this gene product is uniquely dedicated to peptidoglycan binding (Buist et al. 2008).”
Contractile injection systems of bacteriophages and related systems (2018, background): “LysM domains are widely distributed in proteins that bind to (peptido)glycans (Buist et al., 2008) but in gp53 this domain does not display any potential sugar binding interfaces (Taylor et al., 2016).”
Coagulase-Negative Staphylococci (2014, background): “Aae has a modular structure and harbors three repeats in its N-terminal domain, each having high similarity with the lysine motif (LysM), which confers cell wall attachment to various surface-associated proteins (263).”