3cf5

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[[Image:3cf5.png|left|200px]]
 
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==Thiopeptide antibiotic Thiostrepton bound to the large ribosomal subunit of Deinococcus radiodurans==
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The line below this paragraph, containing "STRUCTURE_3cf5", creates the "Structure Box" on the page.
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<StructureSection load='3cf5' size='340' side='right'caption='[[3cf5]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3cf5]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans] and [https://en.wikipedia.org/wiki/Streptomyces_azureus Streptomyces azureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CF5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CF5 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=MG:MAGNESIUM+ION'>MG</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>
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{{STRUCTURE_3cf5| PDB=3cf5 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3cf5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cf5 OCA], [https://pdbe.org/3cf5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cf5 RCSB], [https://www.ebi.ac.uk/pdbsum/3cf5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cf5 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RL33_DEIRA RL33_DEIRA] Binds the 23S rRNA and the E site tRNA.[HAMAP-Rule:MF_00294]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cf/3cf5_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3cf5 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The thiopeptide class of antibiotics targets the GTPase-associated center (GAC) of the ribosome to inhibit translation factor function. Using X-ray crystallography, we have determined the binding sites of thiostrepton (Thio), nosiheptide (Nosi), and micrococcin (Micro), on the Deinococcus radiodurans large ribosomal subunit. The thiopeptides, by binding within a cleft located between the ribosomal protein L11 and helices 43 and 44 of the 23S rRNA, overlap with the position of domain V of EF-G, thus explaining how this class of drugs perturbs translation factor binding to the ribosome. The presence of Micro leads to additional density for the C-terminal domain (CTD) of L7, adjacent to and interacting with L11. The results suggest that L11 acts as a molecular switch to control L7 binding and plays a pivotal role in positioning one L7-CTD monomer on the G' subdomain of EF-G to regulate EF-G turnover during protein synthesis.
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===Thiopeptide antibiotic Thiostrepton bound to the large ribosomal subunit of Deinococcus radiodurans===
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Translational regulation via L11: molecular switches on the ribosome turned on and off by thiostrepton and micrococcin.,Harms JM, Wilson DN, Schluenzen F, Connell SR, Stachelhaus T, Zaborowska Z, Spahn CM, Fucini P Mol Cell. 2008 Apr 11;30(1):26-38. PMID:18406324<ref>PMID:18406324</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The line below this paragraph, {{ABSTRACT_PUBMED_18406324}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3cf5" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 18406324 is the PubMed ID number.
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{{ABSTRACT_PUBMED_18406324}}
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==About this Structure==
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[[3cf5]] is a 31 chain structure of [[Ribosomal protein L11]], [[Ribosomal protein L13]], [[Ribosomal protein L14]], [[Ribosomal protein L15]], [[Ribosomal protein L16]], [[Ribosomal protein L17]], [[Ribosomal protein L18]], [[Ribosomal protein L19]], [[Ribosomal protein L2]], [[Ribosomal protein L20]], [[Ribosomal protein L21]], [[Ribosomal protein L22]], [[Ribosomal protein L23]], [[Ribosomal protein L24]], [[Ribosomal protein L25]], [[Ribosomal protein L27]], [[Ribosomal protein L28]], [[Ribosomal protein L29]], [[Ribosomal protein L3]], [[Ribosomal protein L30]], [[Ribosomal protein L32]], [[Ribosomal protein L33]], [[Ribosomal protein L34]], [[Ribosomal protein L35]], [[Ribosomal protein L36]], [[Ribosomal protein L4]], [[Ribosomal protein L5]], [[Ribosomal protein L6]] and [[Ribosome]] with sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans] and [http://en.wikipedia.org/wiki/Streptomyces_azureus Streptomyces azureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CF5 OCA].
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==See Also==
==See Also==
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*[[Ribosomal protein L11]]
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*[[Ribosome 3D structures|Ribosome 3D structures]]
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*[[Ribosomal protein L13]]
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== References ==
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*[[Ribosomal protein L14]]
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<references/>
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*[[Ribosomal protein L15]]
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__TOC__
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*[[Ribosomal protein L16]]
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</StructureSection>
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*[[Ribosomal protein L17]]
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*[[Ribosomal protein L18]]
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*[[Ribosomal protein L19]]
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*[[Ribosomal protein L2]]
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*[[Ribosomal protein L20]]
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*[[Ribosomal protein L21]]
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*[[Ribosomal protein L22]]
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*[[Ribosomal protein L23]]
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*[[Ribosomal protein L24]]
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*[[Ribosomal protein L25]]
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*[[Ribosomal protein L27]]
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*[[Ribosomal protein L28]]
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*[[Ribosomal protein L29]]
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*[[Ribosomal protein L3]]
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*[[Ribosomal protein L30]]
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*[[Ribosomal protein L32]]
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*[[Ribosomal protein L33]]
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*[[Ribosomal protein L34]]
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*[[Ribosomal protein L35]]
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*[[Ribosomal protein L36]]
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*[[Ribosomal protein L4]]
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*[[Ribosomal protein L5]]
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*[[Ribosomal protein L6]]
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*[[Ribosome]]
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==Reference==
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<ref group="xtra">PMID:018406324</ref><references group="xtra"/>
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[[Category: Deinococcus radiodurans]]
[[Category: Deinococcus radiodurans]]
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[[Category: Large Structures]]
[[Category: Streptomyces azureus]]
[[Category: Streptomyces azureus]]
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[[Category: Connell, S R.]]
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[[Category: Connell SR]]
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[[Category: Fucini, P.]]
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[[Category: Fucini P]]
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[[Category: Harms, J M.]]
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[[Category: Harms JM]]
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[[Category: Schluenzen, F.]]
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[[Category: Schluenzen F]]
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[[Category: Spahn, C M.T.]]
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[[Category: Spahn CMT]]
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[[Category: Stachelhaus, T.]]
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[[Category: Stachelhaus T]]
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[[Category: Wilson, D N.]]
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[[Category: Wilson DN]]
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[[Category: Zaborowska, Z.]]
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[[Category: Zaborowska Z]]
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[[Category: Antibiotic]]
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[[Category: L11]]
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[[Category: Pyridine]]
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[[Category: Ribosome]]
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[[Category: Ribosome-antibiotic complex]]
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[[Category: Rna]]
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[[Category: Thiazole]]
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[[Category: Thiazoline]]
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[[Category: Thiopeptide]]
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[[Category: Thiostrepton]]
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[[Category: Translation inhibition]]
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Current revision

Thiopeptide antibiotic Thiostrepton bound to the large ribosomal subunit of Deinococcus radiodurans

PDB ID 3cf5

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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