4u20: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4u20]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Escherichia_coli_str._K-12_substr._MDS42 Escherichia coli str. K-12 substr. MDS42]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4tou 4tou], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4tov 4tov], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4tow 4tow] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4tox 4tox]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U20 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4U20 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4u20]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Escherichia_coli_str._K-12_substr._MDS42 Escherichia coli str. K-12 substr. MDS42]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4tou 4tou], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4tov 4tov], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4tow 4tow] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4tox 4tox]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U20 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4U20 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=VIF:FLOPRISTIN'>VIF</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=VIF:FLOPRISTIN'>VIF</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4u20 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u20 OCA], [https://pdbe.org/4u20 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4u20 RCSB], [https://www.ebi.ac.uk/pdbsum/4u20 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4u20 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=4u20 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u20 OCA], [https://pdbe.org/4u20 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4u20 RCSB], [https://www.ebi.ac.uk/pdbsum/4u20 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4u20 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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</div> | </div> | ||
<div class="pdbe-citations 4u20" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4u20" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Ribosome 3D structures|Ribosome 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Latest revision as of 03:49, 28 December 2023
Crystal structure of the E. coli ribosome bound to flopristin.Crystal structure of the E. coli ribosome bound to flopristin.
Structural highlights
FunctionPublication Abstract from PubMedStreptogramin antibiotics are divided into type A and B streptogramins, which in combination can act synergistically. We compared the molecular interactions of the streptogramin combinations Synercid (type A: dalfopristin, type B: quinupristin) and NXL 103 (type A: flopristin, type B: linopristin) with the Escherichia coli 70S ribosome by x-ray crystallography. We further analyzed the activity of the streptogramin components individually and in combination. Streptogramin A and B components in Synercid and NXL 103 exhibit synergistic antimicrobial activity against certain pathogenic bacteria. However, in transcription-coupled translation assays, only combinations that include dalfopristin, the streptogramin A component of Synercid, show synergy. Notably, the diethylaminoethylsulfonyl group in dalfopristin reduces its activity, but is the basis for synergy in transcription-coupled translation assays before its rapid hydrolysis from the depsipeptide core. Replacement of the diethylaminoethylsulfonyl group in dalfopristin by a non-hydrolyzable group may therefore be beneficial for synergy. The absence of general streptogramin synergy in transcription-coupled translation assays suggests that synergistic antimicrobial activity of streptogramins can occur independently of streptogramin effects on translation. Synergy of streptogramin antibiotics occurs independently of their effects on translation.,Noeske J, Huang J, Olivier NB, Giacobbe RA, Zambrowski M, Cate JH Antimicrob Agents Chemother. 2014 Jun 23. pii: AAC.03389-14. PMID:24957822[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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