Full metadata record

DC Field Value Language
dc.contributor.authorLee, In Gyun-
dc.contributor.authorSong, Chiman-
dc.contributor.authorYang, Seoyeong-
dc.contributor.authorJeon, Hanul-
dc.contributor.authorPark, Jingyeong-
dc.contributor.authorYoon, Hye Jin-
dc.contributor.authorIm, Hookang-
dc.contributor.authorKang, Sung Min-
dc.contributor.authorEun, Hyun Jong-
dc.contributor.authorLee, Bong Jin-
dc.date.accessioned2024-01-19T12:30:12Z-
dc.date.available2024-01-19T12:30:12Z-
dc.date.created2022-04-21-
dc.date.issued2022-04-
dc.identifier.issn2059-7983-
dc.identifier.urihttps://pubs.kist.re.kr/handle/201004/115461-
dc.description.abstractD-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-Alanylation of teichoic acids is mediated via the action of four proteins encoded by the dlt operon, DltABCD, all four of which are essential for the process. In order to develop novel antimicrobial agents against S. aureus, the D-alanyl carrier protein ligase DltA, which is the first protein in the D-alanylation pathway, was focused on. Here, the crystal structure of DltA from the methicillin-resistant S. aureus strain Mu50 is presented, which reveals the unique molecular details of the catalytic center and the role of the P-loop. Kinetic analysis shows that the enantioselectivity of S. aureus DltA is much higher than that of DltA from other species. In the presence of DltC, the enzymatic activity of DltA is increased by an order of magnitude, suggesting a new exploitable binding pocket. This discovery may pave the way for a new generation of treatments for drug-resistant S. aureus.-
dc.languageEnglish-
dc.publisherINT UNION CRYSTALLOGRAPHY-
dc.titleStructural and functional analysis of the D-alanyl carrier protein ligase DltA from Staphylococcus aureus Mu50-
dc.typeArticle-
dc.identifier.doi10.1107/S2059798322000547-
dc.description.journalClass1-
dc.identifier.bibliographicCitationActa Crystallographica Section D - Structural Biology, v.78, pp.424 - 434-
dc.citation.titleActa Crystallographica Section D - Structural Biology-
dc.citation.volume78-
dc.citation.startPage424-
dc.citation.endPage434-
dc.description.isOpenAccessY-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.identifier.wosid000777860500003-
dc.relation.journalWebOfScienceCategoryBiochemical Research Methods-
dc.relation.journalWebOfScienceCategoryBiochemistry & Molecular Biology-
dc.relation.journalWebOfScienceCategoryBiophysics-
dc.relation.journalWebOfScienceCategoryCrystallography-
dc.relation.journalResearchAreaBiochemistry & Molecular Biology-
dc.relation.journalResearchAreaBiophysics-
dc.relation.journalResearchAreaCrystallography-
dc.type.docTypeArticle-
dc.subject.keywordPlusTEICHOIC-ACIDS-
dc.subject.keywordPlusCRYSTAL-STRUCTURE-
dc.subject.keywordPlusRESISTANCE-
dc.subject.keywordPlusCOLONIZATION-
dc.subject.keywordPlusSUSCEPTIBILITY-
dc.subject.keywordPlusBIOSYNTHESIS-
dc.subject.keywordPlusINHIBITION-
dc.subject.keywordPlusVANCOMYCIN-
dc.subject.keywordPlusSEQUENCE-
dc.subject.keywordPlusTARGET-
dc.subject.keywordAuthorStaphylococcus aureus-
dc.subject.keywordAuthordlt operon-
dc.subject.keywordAuthorD-alanyl carrier protein ligase DltA-
Appears in Collections:
KIST Article > 2022
Files in This Item:
There are no files associated with this item.
Export
RIS (EndNote)
XLS (Excel)
XML

qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

BROWSE