Payne_2009_Mol.Microbiol_73_367

Reference

Title : Mycobacteriophage Lysin B is a novel mycolylarabinogalactan esterase - Payne_2009_Mol.Microbiol_73_367
Author(s) : Payne K , Sun Q , Sacchettini J , Hatfull GF
Ref : Molecular Microbiology , 73 :367 , 2009
Abstract :

Mycobacteriophages encounter a unique problem among phages of Gram-positive bacteria, in that lysis must not only degrade the peptidoglycan layer but also circumvent a mycolic acid-rich outer membrane covalently attached to the arabinogalactan-peptidoglycan complex. Mycobacteriophages accomplish this by producing two lysis enzymes, Lysin A (LysA) that hydrolyses peptidoglycan, and Lysin B (LysB), a novel mycolylarabinogalactan esterase, that cleaves the mycolylarabinogalactan bond to release free mycolic acids. The D29 LysB structure shows an alpha/beta hydrolase organization with a catalytic triad common to cutinases, but which contains an additional four-helix domain implicated in the binding of lipid substrates. Whereas LysA is essential for mycobacterial lysis, a Giles DeltalysB mutant mycobacteriophage is viable, but defective in the normal timing, progression and completion of host cell lysis. We propose that LysB facilitates lysis by compromising the integrity of the mycobacterial outer membrane linkage to the arabinogalactan-peptidoglycan layer.

PubMedSearch : Payne_2009_Mol.Microbiol_73_367
PubMedID: 19555454
Gene_locus related to this paper: bpmd2-vg12

Related information

Gene_locus bpmd2-vg12
Family Lysin_B_C_ter    Cutinase
Structure 3HC7

Citations formats

Payne K, Sun Q, Sacchettini J, Hatfull GF (2009)
Mycobacteriophage Lysin B is a novel mycolylarabinogalactan esterase
Molecular Microbiology 73 :367

Payne K, Sun Q, Sacchettini J, Hatfull GF (2009)
Molecular Microbiology 73 :367