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<SX load='3j25' size='340' side='right' viewer='molstar' caption='[[3j25]], [[Resolution|resolution]] 7.20&Aring;' scene=''>
<SX load='3j25' size='340' side='right' viewer='molstar' caption='[[3j25]], [[Resolution|resolution]] 7.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3j25]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"enterococcus_proteiformis"_thiercelin_and_jouhaud_1903 "enterococcus proteiformis" thiercelin and jouhaud 1903]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J25 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J25 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3j25]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J25 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J25 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GCP:PHOSPHOMETHYLPHOSPHONIC+ACID+GUANYLATE+ESTER'>GCP</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 7.2&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tetM, transposon TnFO1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1351 "Enterococcus proteiformis" Thiercelin and Jouhaud 1903])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GCP:PHOSPHOMETHYLPHOSPHONIC+ACID+GUANYLATE+ESTER'>GCP</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=3j25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j25 OCA], [https://pdbe.org/3j25 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j25 RCSB], [https://www.ebi.ac.uk/pdbsum/3j25 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j25 ProSAT]</span></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=3j25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j25 OCA], [https://pdbe.org/3j25 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j25 RCSB], [https://www.ebi.ac.uk/pdbsum/3j25 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j25 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/TET1_ENTFL TET1_ENTFL]] Abolishes the inhibitory effect of tetracyclin on protein synthesis by a non-covalent modification of the ribosomes.  
[https://www.uniprot.org/uniprot/TET1_ENTFL TET1_ENTFL] Abolishes the inhibitory effect of tetracyclin on protein synthesis by a non-covalent modification of the ribosomes.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ribosome protection proteins (RPPs) confer tetracycline resistance by binding to the ribosome and chasing the drug from its binding site. The current model for the mechanism of action of RPPs proposes that drug release is indirect and achieved via conformational changes within the drug-binding site induced upon binding of the RPP to the ribosome. Here we report a cryo-EM structure of the RPP TetM in complex with the 70S ribosome at 7.2-A resolution. The structure reveals the contacts of TetM with the ribosome, including interaction between the conserved and functionally critical C-terminal extension of TetM and the decoding center of the small subunit. Moreover, we observe direct interaction between domain IV of TetM and the tetracycline binding site and identify residues critical for conferring tetracycline resistance. A model is presented whereby TetM directly dislodges tetracycline to confer resistance.
 
Structural basis for TetM-mediated tetracycline resistance.,Donhofer A, Franckenberg S, Wickles S, Berninghausen O, Beckmann R, Wilson DN Proc Natl Acad Sci U S A. 2012 Oct 1. PMID:23027944<ref>PMID:23027944</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3j25" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</SX>
</SX>
[[Category: Enterococcus proteiformis thiercelin and jouhaud 1903]]
[[Category: Enterococcus faecalis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Beckmann, R]]
[[Category: Beckmann R]]
[[Category: Berninghausen, O]]
[[Category: Berninghausen O]]
[[Category: Doenhoefer, A]]
[[Category: Doenhoefer A]]
[[Category: Franckenberg, S]]
[[Category: Franckenberg S]]
[[Category: Wickles, S]]
[[Category: Wickles S]]
[[Category: Wilson, D N]]
[[Category: Wilson DN]]
[[Category: Antibiotic resistance]]
[[Category: Translation]]

Latest revision as of 10:09, 21 February 2024

Structural basis for TetM-mediated tetracycline resistance

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