This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


3j5l

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: '''Unreleased structure''' The entry 3j5l is ON HOLD Authors: Arenz S, Berninghausen O, Beckmann R, Wilson DN Description: Structure of the E. coli 50S subunit with ErmBL nascent chain)
Current revision (14:15, 24 January 2024) (edit) (undo)
 
(10 intermediate revisions not shown.)
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 3j5l is ON HOLD
+
==Structure of the E. coli 50S subunit with ErmBL nascent chain==
 +
<SX load='3j5l' size='340' side='right' viewer='molstar' caption='[[3j5l]], [[Resolution|resolution]] 6.60&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[3j5l]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Streptococcus_sanguinis Streptococcus sanguinis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J5L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J5L FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 6.6&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ERY:ERYTHROMYCIN+A'>ERY</scene>, <scene name='pdbligand=MA6:6N-DIMETHYLADENOSINE-5-MONOPHOSHATE'>MA6</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</scene></td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3j5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j5l OCA], [https://pdbe.org/3j5l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j5l RCSB], [https://www.ebi.ac.uk/pdbsum/3j5l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j5l ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/RL2_ECOLI RL2_ECOLI] One of the primary rRNA binding proteins. Located near the base of the L1 stalk, it is probably also mobile. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is highly controversial.[HAMAP-Rule:MF_01320_B] In the E.coli 70S ribosome in the initiation state it has been modeled to make several contacts with the 16S rRNA (forming bridge B7b, PubMed:12809609); these contacts are broken in the model with bound EF-G.[HAMAP-Rule:MF_01320_B]
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
In bacteria, ribosome stalling during translation of ErmBL leader peptide occurs in the presence of the antibiotic erythromycin and leads to induction of expression of the downstream macrolide resistance methyltransferase ErmB. The lack of structures of drug-dependent stalled ribosome complexes (SRCs) has limited our mechanistic understanding of this regulatory process. Here we present a cryo-electron microscopy structure of the erythromycin-dependent ErmBL-SRC. The structure reveals that the antibiotic does not interact directly with ErmBL, but rather redirects the path of the peptide within the tunnel. Furthermore, we identify a key peptide-ribosome interaction that defines an important relay pathway from the ribosomal tunnel to the peptidyltransferase centre (PTC). The PTC of the ErmBL-SRC appears to adopt an uninduced state that prevents accommodation of Lys-tRNA at the A-site, thus providing structural basis for understanding how the drug and the nascent peptide cooperate to inhibit peptide bond formation and induce translation arrest.
-
Authors: Arenz S, Berninghausen O, Beckmann R, Wilson DN
+
Molecular basis for erythromycin-dependent ribosome stalling during translation of the ErmBL leader peptide.,Arenz S, Ramu H, Gupta P, Berninghausen O, Beckmann R, Vazquez-Laslop N, Mankin AS, Wilson DN Nat Commun. 2014 Mar 24;5:3501. doi: 10.1038/ncomms4501. PMID:24662426<ref>PMID:24662426</ref>
-
Description: Structure of the E. coli 50S subunit with ErmBL nascent chain
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 3j5l" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</SX>
 +
[[Category: Escherichia coli K-12]]
 +
[[Category: Large Structures]]
 +
[[Category: Streptococcus sanguinis]]
 +
[[Category: Arenz S]]
 +
[[Category: Beckmann R]]
 +
[[Category: Berninghausen O]]
 +
[[Category: Gupta P]]
 +
[[Category: Mankin AS]]
 +
[[Category: Ramu H]]
 +
[[Category: Vazquez-Laslop N]]
 +
[[Category: Wilson DN]]

Current revision

Structure of the E. coli 50S subunit with ErmBL nascent chain

3j5l, resolution 6.60Å

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools