Structural basis for HflXr-mediated antibiotic resistance in Listeria monocytogenes
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F22%3A00563901" target="_blank" >RIV/61388963:_____/22:00563901 - isvavai.cz</a>
Result on the web
<a href="https://doi.org/10.1093/nar/gkac934" target="_blank" >https://doi.org/10.1093/nar/gkac934</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1093/nar/gkac934" target="_blank" >10.1093/nar/gkac934</a>
Alternative languages
Result language
angličtina
Original language name
Structural basis for HflXr-mediated antibiotic resistance in Listeria monocytogenes
Original language description
HflX is a ubiquitous bacterial GTPase that splits and recycles stressed ribosomes. In addition to HflX, Listeria monocytogenes contains a second HflX homolog, HflXr. Unlike HflX, HflXr confers resistance to macrolide and lincosamide antibiotics by an experimentally unexplored mechanism. Here, we have determined cryo-EM structures of L. monocytogenes HflXr-50S and HflX-50S complexes as well as L. monocytogenes 70S ribosomes in the presence and absence of the lincosamide lincomycin. While the overall geometry of HflXr on the 50S subunit is similar to that of HflX, a loop within the N-terminal domain of HflXr, which is two amino acids longer than in HflX, reaches deeper into the peptidyltransferase center. Moreover, unlike HflX, the binding of HflXr induces conformational changes within adjacent rRNA nucleotides that would be incompatible with drug binding. These findings suggest that HflXr confers resistance using an allosteric ribosome protection mechanism, rather than by simply splitting and recycling antibiotic-stalled ribosomes.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10606 - Microbiology
Result continuities
Project
—
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2022
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Nucleic Acids Research
ISSN
0305-1048
e-ISSN
1362-4962
Volume of the periodical
50
Issue of the periodical within the volume
19
Country of publishing house
GB - UNITED KINGDOM
Number of pages
16
Pages from-to
11285-11300
UT code for WoS article
000873820100001
EID of the result in the Scopus database
2-s2.0-85144543997