Structural insight into the antibiotic action of telithromycin against resistant mutants

Rita Berisio; Joerg Harms; Frank Schluenzen; Raz Zarivach; Harly A.S. Hansen; Paola Fucini; Ada Yonath

doi:10.1128/JB.185.14.4276-4279.2003

Structural insight into the antibiotic action of telithromycin against resistant mutants

Rita Berisio
, Joerg Harms
, Frank Schluenzen
, Raz Zarivach
, Harly A.S. Hansen
, Paola Fucini
, Ada Yonath

Research output: Contribution to journal › Article › peer-review

168 Scopus citations

Abstract

The crystal structure of the ketolide telithromycin bound to the Deinococcus radiodurans large ribosomal subunit shows that telithromycin blocks the ribosomal exit tunnel and interacts with domains II and V of the 23S RNA. Comparisons to other clinically relevant macrolides provided structural insights into its enhanced activity against macrolide-resistant strains.

Original language	English
Pages (from-to)	4276-4279
Number of pages	4
Journal	Journal of Bacteriology
Volume	185
Issue number	14
DOIs	https://doi.org/10.1128/JB.185.14.4276-4279.2003
State	Published - 1 Jul 2003
Externally published	Yes

ASJC Scopus subject areas

Microbiology
Molecular Biology

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10.1128/JB.185.14.4276-4279.2003

Cite this

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abstract = "The crystal structure of the ketolide telithromycin bound to the Deinococcus radiodurans large ribosomal subunit shows that telithromycin blocks the ribosomal exit tunnel and interacts with domains II and V of the 23S RNA. Comparisons to other clinically relevant macrolides provided structural insights into its enhanced activity against macrolide-resistant strains.",

author = "Rita Berisio and Joerg Harms and Frank Schluenzen and Raz Zarivach and Hansen, \{Harly A.S.\} and Paola Fucini and Ada Yonath",

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AU - Berisio, Rita

AU - Harms, Joerg

AU - Schluenzen, Frank

AU - Zarivach, Raz

AU - Hansen, Harly A.S.

AU - Fucini, Paola

AU - Yonath, Ada

PY - 2003/7/1

Y1 - 2003/7/1

N2 - The crystal structure of the ketolide telithromycin bound to the Deinococcus radiodurans large ribosomal subunit shows that telithromycin blocks the ribosomal exit tunnel and interacts with domains II and V of the 23S RNA. Comparisons to other clinically relevant macrolides provided structural insights into its enhanced activity against macrolide-resistant strains.

AB - The crystal structure of the ketolide telithromycin bound to the Deinococcus radiodurans large ribosomal subunit shows that telithromycin blocks the ribosomal exit tunnel and interacts with domains II and V of the 23S RNA. Comparisons to other clinically relevant macrolides provided structural insights into its enhanced activity against macrolide-resistant strains.

UR - https://www.scopus.com/pages/publications/0038492422

U2 - 10.1128/JB.185.14.4276-4279.2003

DO - 10.1128/JB.185.14.4276-4279.2003

M3 - Article

C2 - 12837804

AN - SCOPUS:0038492422

SN - 0021-9193

VL - 185

SP - 4276

EP - 4279

JO - Journal of Bacteriology

JF - Journal of Bacteriology

IS - 14

ER -

Structural insight into the antibiotic action of telithromycin against resistant mutants

Abstract

ASJC Scopus subject areas

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