4u1v: Difference between revisions
New page: '''Unreleased structure''' The entry 4u1v is ON HOLD Authors: Noeske, J., Huang, J., Olivier, N.B., Giacobbe, R.A., Zambrowski, M., Cate, J.H.D. Description: Crystal structure of the E... |
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==Crystal structure of the E. coli ribosome bound to linopristin.== | |||
<StructureSection load='4u1v' size='340' side='right'caption='[[4u1v]], [[Resolution|resolution]] 3.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4u1v]] 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=4tol 4tol], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4tom 4tom], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4ton 4ton] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4too 4too]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U1V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4U1V FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=004:(2S)-AMINO(PHENYL)ETHANOIC+ACID'>004</scene>, <scene name='pdbligand=04X:(2S)-5-(MORPHOLIN-4-YLMETHYL)-1,2,3,6-TETRAHYDROPYRIDINE-2-CARBOXYLIC+ACID'>04X</scene>, <scene name='pdbligand=DBB:D-ALPHA-AMINOBUTYRIC+ACID'>DBB</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MHU:4-N,N-(DIMETHYLAMINO)-L-PHENYLALANINE'>MHU</scene>, <scene name='pdbligand=MHW:3-HYDROXYPICOLINIC+ACID'>MHW</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=4u1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u1v OCA], [https://pdbe.org/4u1v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4u1v RCSB], [https://www.ebi.ac.uk/pdbsum/4u1v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4u1v ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/RS2_ECOLI RS2_ECOLI] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Streptogramin 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<ref>PMID:24957822</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4u1v" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ribosome 3D structures|Ribosome 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli K-12]] | |||
[[Category: Escherichia coli str. K-12 substr. MDS42]] | |||
[[Category: Large Structures]] | |||
[[Category: Cate JHD]] | |||
[[Category: Giacobbe RA]] | |||
[[Category: Huang J]] | |||
[[Category: Noeske J]] | |||
[[Category: Olivier NB]] | |||
[[Category: Zambrowski M]] | |||
Latest revision as of 03:49, 28 December 2023
Crystal structure of the E. coli ribosome bound to linopristin.Crystal structure of the E. coli ribosome bound to linopristin.
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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