2022
DOI: 10.1107/s2059798322000547
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Structural and functional analysis of the D-alanyl carrier protein ligase DltA from Staphylococcus aureus Mu50

Abstract: D-Alanylation of the teichoic acids of the Gram-positive bacterial cell wall plays crucial roles in bacterial physiology and virulence. Deprivation of D-alanine from the teichoic acids of Staphylococcus aureus impairs biofilm and colony formation, induces autolysis and ultimately renders methicillin-resistant S. aureus highly susceptible to antimicrobial agents and host defense peptides. Hence, the D-alanylation pathway has emerged as a promising antibacterial target against drug-resistant S. aureus. D-Alanyla… Show more

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Cited by 4 publications
(3 citation statements)
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“…Despite AlmE displaying promiscuity for D-Ala activation, this residue was never successfully transferred to the downstream T domain, and crystals could not be obtained with the replacement of Gly with D-Ala. 61 Indeed, DltA displays an increased affinity for its native substrate D-Ala, and concomitant decreased affinity for L-Ala, in the presence of coenzyme A (CoA) as a Ppant mimic or its cognate Ppant-modied T domain. 25,75 2…”
Section: Structural Analysismentioning
confidence: 99%
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“…Despite AlmE displaying promiscuity for D-Ala activation, this residue was never successfully transferred to the downstream T domain, and crystals could not be obtained with the replacement of Gly with D-Ala. 61 Indeed, DltA displays an increased affinity for its native substrate D-Ala, and concomitant decreased affinity for L-Ala, in the presence of coenzyme A (CoA) as a Ppant mimic or its cognate Ppant-modied T domain. 25,75 2…”
Section: Structural Analysismentioning
confidence: 99%
“…72 This is reminiscent of the glycylation of lipopolysaccharides described above, and moreover, AlmE shows both active site similarity to DltA and relaxed substrate selectivity towards d -Ala. 61 DltA has been crystallized several times from various organisms, and separate investigations of the active site binding pocket broadly corroborate each other. 20,25,73–76 The first of these reports identified several residues important for coordination of both the α-amino group (D197, G295 and V301) and the d -methyl group (L198 and C269) in the Bacillus cereus -derived enzyme (Fig. 7A).…”
Section: Structural Analysismentioning
confidence: 99%
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