1oln

From Proteopedia

(Difference between revisions)

Revision as of 09:54, 26 May 2021

Model for thiostrepton antibiotic binding to L11 substrate from 50S ribosomal RNA

Structural highlights

1oln is a 3 chain structure with sequence from Streptomyces azureus and Thermotoga maritima. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:	, , , , , , ,
Related:	1d8t, 1e9w, 2c77, 2jq7, 2zjp, 3cf5, 1mms, 1eg0, 1giy, 1jqm, 1jqs, 1jqt, 1pn7, 1pn8, 487d
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RL11_THEMA] This protein binds directly to 23S ribosomal RNA. [THCL_STRAJ] Has bacteriocidal activity. Inhibits bacterial protein biosynthesis by acting on the elongation factor Tu (EF-Tu) (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Thiostrepton and micrococcin inhibit protein synthesis by binding to the L11 binding domain (L11BD) of 23S ribosomal RNA. The two compounds are structurally related, yet they produce different effects on ribosomal RNA in footprinting experiments and on elongation factor-G (EF-G)-dependent GTP hydrolysis. Using NMR and an assay based on A1067 methylation by thiostrepton-resistance methyltransferase, we show that the related thiazoles, nosiheptide and siomycin, also bind to this region. The effect of all four antibiotics on EF-G-dependent GTP hydrolysis and EF-G-GDP-ribosome complex formation was studied. Our NMR and biochemical data demonstrate that thiostrepton, nosiheptide, and siomycin share a common profile, which differs from that of micrococcin. We have generated a three-dimensional (3D) model for the interaction of thiostrepton with L11BD RNA. The model rationalizes the differences between micrococcin and the thiostrepton-like antibiotics interacting with L11BD.

Structural basis for contrasting activities of ribosome binding thiazole antibiotics.,Lentzen G, Klinck R, Matassova N, Aboul-ela F, Murchie AI Chem Biol. 2003 Aug;10(8):769-78. PMID:12954336^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Lentzen G, Klinck R, Matassova N, Aboul-ela F, Murchie AI. Structural basis for contrasting activities of ribosome binding thiazole antibiotics. Chem Biol. 2003 Aug;10(8):769-78. PMID:12954336

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1oln"

@@ Line 3: / Line 3: @@
 <StructureSection load='1oln' size='340' side='right'caption='[[1oln]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1oln]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_azureus Streptomyces azureus] and [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OLN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OLN FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1oln]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_azureus Streptomyces azureus] and [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OLN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OLN FirstGlance]. <br>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=BB9:(2Z)-2-AMINO-3-SULFANYLPROP-2-ENOIC+ACID'>BB9</scene>, <scene name='pdbligand=DBU:(2Z)-2-AMINOBUT-2-ENOIC+ACID'>DBU</scene>, <scene name='pdbligand=DCY:D-CYSTEINE'>DCY</scene>, <scene name='pdbligand=DHA:2-AMINO-ACRYLIC+ACID'>DHA</scene>, <scene name='pdbligand=MH6:3-HYDROXY-2-IMINOPROPANOIC+ACID'>MH6</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=QUA:8-HYDROXY-4-(1-HYDROXYETHYL)QUINOLINE-2-CARBOXYLIC+ACID'>QUA</scene>, <scene name='pdbligand=TS9:(2S,3S,4R)-2-AMINO-3,4-DIHYDROXY-3-METHYLPENTANOIC+ACID'>TS9</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1d8t|1d8t]], [[1e9w|1e9w]], [[2c77|2c77]], [[2jq7|2jq7]], [[2zjp|2zjp]], [[3cf5|3cf5]], [[1mms|1mms]], [[1eg0|1eg0]], [[1giy|1giy]], [[1jqm|1jqm]], [[1jqs|1jqs]], [[1jqt|1jqt]], [[1pn7|1pn7]], [[1pn8|1pn8]], [[487d|487d]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1d8t|1d8t]], [[1e9w|1e9w]], [[2c77|2c77]], [[2jq7|2jq7]], [[2zjp|2zjp]], [[3cf5|3cf5]], [[1mms|1mms]], [[1eg0|1eg0]], [[1giy|1giy]], [[1jqm|1jqm]], [[1jqs|1jqs]], [[1jqt|1jqt]], [[1pn7|1pn7]], [[1pn8|1pn8]], [[487d|487d]]</div></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oln OCA], [http://pdbe.org/1oln PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1oln RCSB], [http://www.ebi.ac.uk/pdbsum/1oln PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1oln 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=1oln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oln OCA], [https://pdbe.org/1oln PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oln RCSB], [https://www.ebi.ac.uk/pdbsum/1oln PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oln ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/RL11_THEMA RL11_THEMA]] This protein binds directly to 23S ribosomal RNA. [[http://www.uniprot.org/uniprot/THCL_STRAJ THCL_STRAJ]] Has bacteriocidal activity. Inhibits bacterial protein biosynthesis by acting on the elongation factor Tu (EF-Tu) (By similarity).
+[[https://www.uniprot.org/uniprot/RL11_THEMA RL11_THEMA]] This protein binds directly to 23S ribosomal RNA. [[https://www.uniprot.org/uniprot/THCL_STRAJ THCL_STRAJ]] Has bacteriocidal activity. Inhibits bacterial protein biosynthesis by acting on the elongation factor Tu (EF-Tu) (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1oln

From Proteopedia

Revision as of 09:54, 26 May 2021

Model for thiostrepton antibiotic binding to L11 substrate from 50S ribosomal RNA

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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