Detailed mutational analysis of Vga(A) interdomain linker: implication for antibiotic resistance specificity and mechanism
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
25512423
PubMed Central
PMC4335903
DOI
10.1128/aac.04468-14
PII: AAC.04468-14
Knihovny.cz E-zdroje
- MeSH
- antibakteriální látky farmakologie MeSH
- bakteriální proteiny genetika metabolismus MeSH
- diterpeny farmakologie MeSH
- elektronová kryomikroskopie MeSH
- linkosamidy farmakologie MeSH
- mikrobiální testy citlivosti MeSH
- mnohočetná bakteriální léková rezistence MeSH
- pleuromutiliny MeSH
- polycyklické sloučeniny MeSH
- ribozomy metabolismus MeSH
- streptograminy farmakologie MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- antibakteriální látky MeSH
- bakteriální proteiny MeSH
- diterpeny MeSH
- linkosamidy MeSH
- polycyklické sloučeniny MeSH
- streptograminy MeSH
Detailed mutational analysis examines the roles of individual residues of the Vga(A) linker in determining the antibiotic resistance phenotype. It defines a narrowed region of residues 212 to 220 whose composition determines the resistance specificity to lincosamides, pleuromutilins, and/or streptogramins A. From the analogy with the recently described function of the homologous ABC-F protein EttA as a translational factor, we infer that the Vga(A) linker interacts with the ribosome and directly or indirectly affects the binding of the respective antibiotic.
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Structural basis for antibiotic resistance mediated by the Bacillus subtilis ABCF ATPase VmlR
PDB
1SM1, 3I9C, 3J5S, 3OFZ