4u26
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the E. coli ribosome bound to dalfopristin and quinupristin.== | |
| + | <StructureSection load='4u26' size='340' side='right'caption='[[4u26]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4u26]] 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=4tp8 4tp8], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4tp9 4tp9], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4tpa 4tpa] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4tpb 4tpb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U26 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4U26 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]] 2.8Å</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=DBB:D-ALPHA-AMINOBUTYRIC+ACID'>DBB</scene>, <scene name='pdbligand=DOL:5-(2-DIETHYLAMINO-ETHANESULFONYL)-21-HYDROXY-10-ISOPROPYL-11,19-DIMETHYL-9,26-DIOXA-3,15,28-TRIAZA-TRICYCLO[23.2.1.00,255]OCTACOSA-1(27),12,17,19,25(28)-PENTAENE-2,8,14,23-TETRAONE'>DOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MHT:(3S)-3-(METHYLSULFANYL)-1-AZABICYCLO[2.2.2]OCTANE'>MHT</scene>, <scene name='pdbligand=MHU:4-N,N-(DIMETHYLAMINO)-L-PHENYLALANINE'>MHU</scene>, <scene name='pdbligand=MHV:4-OXO-L-PIPECOLIC+ACID'>MHV</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=4u26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u26 OCA], [https://pdbe.org/4u26 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4u26 RCSB], [https://www.ebi.ac.uk/pdbsum/4u26 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4u26 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/RS5_ECOLI RS5_ECOLI] With S4 and S12 plays an important role in translational accuracy. Many suppressors of streptomycin-dependent mutants of protein S12 are found in this protein, some but not all of which decrease translational accuracy (ram, ribosomal ambiguity mutations).<ref>PMID:15652481</ref> Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body.<ref>PMID:15652481</ref> The physical location of this protein suggests it may also play a role in mRNA unwinding by the ribosome, possibly by forming part of a processivity clamp.<ref>PMID:15652481</ref> | ||
| + | <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 4u26" 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]] | ||
Current revision
Crystal structure of the E. coli ribosome bound to dalfopristin and quinupristin.
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