scholarly journals Structural Insights into the Functions of the Large Ribosomal Subunit, a Major Antibiotic Target

2008 ◽  
Vol 57 (1) ◽  
pp. 1-14 ◽  
Author(s):  
Thomas A. Steitz
Keyword(s):  
Ribosomal Subunit ◽  
Large Ribosomal Subunit ◽  
Subunit A ◽  
Antibiotic Target ◽  
Structural Insights

scholarly journals Structural insights into species-specific features of the ribosome from the pathogen Staphylococcus aureus

2015 ◽  
Vol 112 (43) ◽  
pp. E5805-E5814 ◽  
Author(s):  
Zohar Eyal ◽  
Donna Matzov ◽  
Miri Krupkin ◽  
Itai Wekselman ◽  
Susanne Paukner ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Staphylococcus Aureus ◽  
Ribosomal Subunit ◽  
Binding Modes ◽  
Large Ribosomal Subunit ◽  
Structural Motifs ◽  
Antibiotic Drugs ◽  
Species Specific ◽  
Structural Insights ◽  
Shed Light

The emergence of bacterial multidrug resistance to antibiotics threatens to cause regression to the preantibiotic era. Here we present the crystal structure of the large ribosomal subunit from Staphylococcus aureus, a versatile Gram-positive aggressive pathogen, and its complexes with the known antibiotics linezolid and telithromycin, as well as with a new, highly potent pleuromutilin derivative, BC-3205. These crystal structures shed light on specific structural motifs of the S. aureus ribosome and the binding modes of the aforementioned antibiotics. Moreover, by analyzing the ribosome structure and comparing it with those of nonpathogenic bacterial models, we identified some unique internal and peripheral structural motifs that may be potential candidates for improving known antibiotics and for use in the design of selective antibiotic drugs against S. aureus.

scholarly journals Structural Insight into the Antibiotic Action of Telithromycin against Resistant Mutants

2003 ◽  
Vol 185 (14) ◽  
pp. 4276-4279 ◽  
Author(s):  
Rita Berisio ◽  
Joerg Harms ◽  
Frank Schluenzen ◽  
Raz Zarivach ◽  
Harly A. S. Hansen ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Deinococcus Radiodurans ◽  
Ribosomal Subunit ◽  
Large Ribosomal Subunit ◽  
Resistant Strains ◽  
Structural Insight ◽  
Resistant Mutants ◽  
Exit Tunnel ◽  
Structural Insights ◽  
Insight Into

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.

scholarly journals High Resolution Structure of the Large Ribosomal Subunit from a Mesophilic Eubacterium

Cell ◽  
2001 ◽  
Vol 107 (5) ◽  
pp. 679-688 ◽  
Author(s):  
Joerg Harms ◽  
Frank Schluenzen ◽  
Raz Zarivach ◽  
Anat Bashan ◽  
Sharon Gat ◽  
...  
Keyword(s):  
High Resolution ◽  
Ribosomal Subunit ◽  
Large Ribosomal Subunit ◽  
High Resolution Structure ◽  
Resolution Structure

scholarly journals A single N1-methyladenosine on the large ribosomal subunit rRNA impacts locally its structure and the translation of key metabolic enzymes

2018 ◽  
Vol 8 (1) ◽  
Author(s):  
Sunny Sharma ◽  
Johannes David Hartmann ◽  
Peter Watzinger ◽  
Arvid Klepper ◽  
Christian Peifer ◽  
...  
Keyword(s):  
Ribosomal Subunit ◽  
Metabolic Enzymes ◽  
Large Ribosomal Subunit

scholarly journals The enigmatic ribosomal stalk

2018 ◽  
Vol 51 ◽  
Author(s):  
Anders Liljas ◽  
Suparna Sanyal
Keyword(s):  
Early Phase ◽  
Ribosomal Subunit ◽  
Structure And Function ◽  
Large Ribosomal Subunit ◽  
Translation Factors ◽  
Ribosomal Stalk ◽  
And Function ◽  
High Degree

Abstract The large ribosomal subunit has a distinct feature, the stalk, extending outside the ribosome. In bacteria it is called the L12 stalk. The base of the stalk is protein uL10 to which two or three dimers of proteins bL12 bind. In archea and eukarya P1 and P2 proteins constitute the stalk. All these extending proteins, that have a high degree of flexibility due to a hinge between their N- and C-terminal parts, are essential for proper functionalization of some of the translation factors. The role of the stalk proteins has remained enigmatic for decades but is gradually approaching an understanding. In this review we summarise the knowhow about the structure and function of the ribosomal stalk till date starting from the early phase of ribosome research.

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