scholarly journals Crystal structure of RlmM, the 2′O-ribose methyltransferase for C2498 of Escherichia coli 23S rRNA

2012 ◽  
Vol 40 (20) ◽  
pp. 10507-10520 ◽  
Author(s):  
Avinash S. Punekar ◽  
Tyson R. Shepherd ◽  
Josefine Liljeruhm ◽  
Anthony C. Forster ◽  
Maria Selmer
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
23S Rrna

scholarly journals Mutations in the GTPase Center of Escherichia coli 23S rRNA Indicate Release Factor 2-Interactive Sites

2002 ◽  
Vol 184 (4) ◽  
pp. 1200-1203 ◽  
Author(s):  
Wenbing Xu ◽  
Frances T. Pagel ◽  
Emanuel J. Murgola
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
Translation Termination ◽  
23S Rrna ◽  
Release Factor ◽  
Suppressor Activity ◽  
Suppressor Mutations ◽  
Nonsense Suppressors

ABSTRACT Mutations in the GTPase center of Escherichia coli 23S rRNA were characterized in vivo as UGA-specific nonsense suppressors. Some site-directed mutations did not exhibit suppressor activity and were interspersed among suppressor mutations. Our results demonstrate the involvement of the two adjacent loops of this conserved rRNA structure in UGA-dependent translation termination and, taken with previous in vitro analyses and with consideration of the crystal structure of the GTPase center RNA, indicate that nucleotides 1067, 1093, 1094, and 1095 are sites of interaction with release factor 2.

Crystal Structure of Murein-Tripeptide Amidase MpaA from Escherichia coli O157 at 2.6 Å Resolution

2017 ◽  
Vol 24 (2) ◽  
pp. 181-187 ◽  
Author(s):  
Yinliang Ma ◽  
Guohui Bai ◽  
Yaqi Cui ◽  
Jing Zhao ◽  
Zenglin Yuan ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
Escherichia Coli O157

scholarly journals Crystal Structure of the B Subunit of Escherichia coli Heat-labile Enterotoxin Carrying Peptides with Anti-herpes Simplex Virus Type 1 Activity

1999 ◽  
Vol 274 (13) ◽  
pp. 8764-8769
Author(s):  
Dubravka Matković-Calogović ◽  
Arianna Loregian ◽  
Maria Rosa D'Acunto ◽  
Roberto Battistutta ◽  
Alessandro Tossi ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
B Subunit ◽  
Heat Labile ◽  
Simplex Virus

scholarly journals The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5-A resolution.

1994 ◽  
Vol 269 (14) ◽  
pp. 10883-10890 ◽  
Author(s):  
W.T. Wolodko ◽  
M.E. Fraser ◽  
M.N. James ◽  
W.A. Bridger
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
Succinyl Coa Synthetase

scholarly journals Crystal structure of phenylalanine-regulated 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli

Structure ◽  
1999 ◽  
Vol 7 (7) ◽  
pp. 865-875 ◽  
Author(s):  
Igor A Shumilin ◽  
Robert H Kretsinger ◽  
Ronald H Bauerle
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
Phosphate Synthase

scholarly journals The crystal structure and oligomeric form of Escherichia coli l , d -carboxypeptidase A

2018 ◽  
Vol 499 (3) ◽  
pp. 594-599 ◽  
Author(s):  
Karen Meyer ◽  
Christine Addy ◽  
Satoko Akashi ◽  
David I. Roper ◽  
Jeremy R.H. Tame
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
Carboxypeptidase A ◽  
Oligomeric Form

scholarly journals Binding Site of the Bridged Macrolides in the Escherichia coli Ribosome

2005 ◽  
Vol 49 (1) ◽  
pp. 281-288 ◽  
Author(s):  
Liqun Xiong ◽  
Yakov Korkhin ◽  
Alexander S. Mankin
Keyword(s):  
Escherichia Coli ◽  
Tight Binding ◽  
Dimethyl Sulfate ◽  
23S Rrna ◽  
Side Chain ◽  
Macrolide Antibiotics ◽  
Side Chains ◽  
Alkyl Aryl ◽  
E Coli ◽  
Exit Tunnel

ABSTRACT Ketolides represent the latest group of macrolide antibiotics. Tight binding of ketolides to the ribosome appears to correlate with the presence of an extended alkyl-aryl side chain. Recently developed 6,11-bridged bicyclic ketolides extend the spectrum of platforms used to generate new potent macrolides with extended alkyl-aryl side chains. The purpose of the present study was to characterize the site of binding and the action of bridged macrolides in the ribosomes of Escherichia coli. All the bridged macrolides investigated efficiently protected A2058 and A2059 in domain V of 23S rRNA from modification by dimethyl sulfate and U2609 from modification by carbodiimide. In addition, bridged macrolides that carry extended alkyl-aryl side chains protruding from the 6,11 bridge protected A752 in helix 35 of domain II of 23S rRNA from modification by dimethyl sulfate. Bridged macrolides efficiently displaced erythromycin from the ribosome in a competition binding assay. The A2058G mutation in 23S rRNA conferred resistance to the bridged macrolides. The U2609C mutation, which renders E. coli resistant to the previously studied ketolides telithromycin and cethromycin, barely affected cell susceptibility to the bridged macrolides used in this study. The results of the biochemical and genetic studies indicate that in the E. coli ribosome, bridged macrolides bind in the nascent peptide exit tunnel at the site previously described for other macrolide antibiotics. The presence of the side chain promotes the formation of specific interactions with the helix 35 of 23S rRNA.

Sign in / Sign up

Export Citation Format

Share Document