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Putative hexameric glycosyltransferase functional unit revealed by the crystal structure of Acinetobacter baumannii MurG

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Title
Putative hexameric glycosyltransferase functional unit revealed by the crystal structure of Acinetobacter baumannii MurG
Other Titles
항생제 내성 병원균 (Acinetobacter baumannii) 이 가지는 항생제 타겟 단백질인 MurG의 hexamer 형태의 결정 구조 분석
Authors
Jung, Kyoung Ho
Kwon, Sunghark
Kim, Chang Min
Lee, Jun Hyuck
Park, Hyun Ho
Subject
ChemistryCrystallographyMaterials Science
Keywords
Acinetobacter baumanniicell-wall peptidoglycan biosynthesiscrystal structureglycosyltransferasesMurGsuperbugs
Issue Date
2021-07
Citation
Kyoung Ho Jung, et al. 2021. "Putative hexameric glycosyltransferase functional unit revealed by the crystal structure of Acinetobacter baumannii MurG". IUCRJ, 8(4): 574-583.
Abstract
Lipid II, the main component of the bacterial cell wall, is synthesized by the addition of UDP-N-acetylglucosamine to the UDP-N-acetylmuramic acid pentapeptide catalyzed by the glycosyltransferase MurG. Owing to its critical role in cell-wall biosynthesis, MurG is considered to be an attractive target for antibacterial agents. Although the Mur family ligases have been extensively studied, the molecular mechanism of the oligomeric scaffolding assembly of MurG remains unclear. In this study, MurG from Acinetobacter baumannii (abMurG), a human pathogen, was characterized and its hexameric crystal structure was unveiled; this is the first homo-oligomeric structure to be described in the MurG family and the Mur family. Homogeneous protein samples were produced for structural studies using size-exclusion chromatography, the absolute molecular mass was calculated via multi-angle light scattering, and protein?protein interactions were analyzed using the PDBePISA server. abMurG was found to form homo-oligomeric complexes in solution, which might serve as functional units for the scaffolding activity of MurG. Furthermore, analysis of this structure revealed the molecular assembly mechanism of MurG. This structural and biochemical study elucidated the homo-oligomerization mechanism of MurG and suggests a new potential antibiotic target on MurG.
URI
https://repository.kopri.re.kr/handle/201206/12976
DOI
http://dx.doi.org/10.1107/S2052252521003729
Type
Article
Station
해당사항없음
Indexed
SCIE
Appears in Collections  
2021-2021, Development of potential candidates as antibiotics based on polar genetic resources (21-21) / Lee, Jun Hyuck (PM21030)
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