3cc7

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{{Large structure}}
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==Structure of Anisomycin resistant 50S Ribosomal Subunit: 23S rRNA mutation C2487U==
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{{STRUCTURE_3cc7| PDB=3cc7 | SCENE= }}
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<StructureSection load='3cc7' size='340' side='right' caption='[[3cc7]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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===Structure of Anisomycin resistant 50S Ribosomal Subunit: 23S rRNA mutation C2487U===
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== Structural highlights ==
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{{ABSTRACT_PUBMED_18455733}}
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<table><tr><td colspan='2'>[[3cc7]] is a 30 chain structure with sequence from [http://en.wikipedia.org/wiki/Haloarcula_marismortui Haloarcula marismortui]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CC7 OCA]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SR:STRONTIUM+ION'>SR</scene><br>
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<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=1MA:6-HYDRO-1-METHYLADENOSINE-5-MONOPHOSPHATE'>1MA</scene>, <scene name='pdbligand=OMG:O2-METHYLGUANOSINE-5-MONOPHOSPHATE'>OMG</scene>, <scene name='pdbligand=OMU:O2-METHYLURIDINE+5-MONOPHOSPHATE'>OMU</scene>, <scene name='pdbligand=PSU:PSEUDOURIDINE-5-MONOPHOSPHATE'>PSU</scene>, <scene name='pdbligand=UR3:3-METHYLURIDINE-5-MONOPHOSHATE'>UR3</scene></td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3cc2|3cc2]], [[3cc4|3cc4]], [[3cce|3cce]], [[3ccj|3ccj]], [[3ccl|3ccl]], [[3ccm|3ccm]], [[3ccq|3ccq]], [[3ccr|3ccr]], [[3ccs|3ccs]], [[3ccu|3ccu]], [[3ccv|3ccv]], [[3cd6|3cd6]]</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3cc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cc7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3cc7 RCSB], [http://www.ebi.ac.uk/pdbsum/3cc7 PDBsum]</span></td></tr>
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<table>
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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/cc/3cc7_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/chain_selection.php?pdb_ID=2ata 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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Eleven mutations that make Haloarcula marismortui resistant to anisomycin, an antibiotic that competes with the amino acid side chains of aminoacyl tRNAs for binding to the A-site cleft of the large ribosomal unit, have been identified in 23S rRNA. The correlation observed between the sensitivity of H. marismortui to anisomycin and the affinity of its large ribosomal subunits for the drug indicates that its response to anisomycin is determined primarily by the binding of the drug to its large ribosomal subunit. The structures of large ribosomal subunits containing resistance mutations show that these mutations can be divided into two classes: (1) those that interfere with specific drug-ribosome interactions and (2) those that stabilize the apo conformation of the A-site cleft of the ribosome relative to its drug-bound conformation. The conformational effects of some mutations of the second kind propagate through the ribosome for considerable distances and are reversed when A-site substrates bind to the ribosome.
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==About this Structure==
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Mutations outside the anisomycin-binding site can make ribosomes drug-resistant.,Blaha G, Gurel G, Schroeder SJ, Moore PB, Steitz TA J Mol Biol. 2008 Jun 6;379(3):505-19. Epub 2008 Apr 8. PMID:18455733<ref>PMID:18455733</ref>
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[[3cc7]] is a 30 chain structure with sequence from [http://en.wikipedia.org/wiki/Haloarcula_marismortui Haloarcula marismortui]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CC7 OCA].
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==See Also==
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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*[[Ribosomal protein L10|Ribosomal protein L10]]
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</div>
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*[[Ribosomal protein L11|Ribosomal protein L11]]
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== References ==
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*[[Ribosomal protein L13|Ribosomal protein L13]]
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<references/>
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*[[Ribosomal protein L14|Ribosomal protein L14]]
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__TOC__
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*[[Ribosomal protein L19|Ribosomal protein L19]]
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</StructureSection>
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*[[Ribosomal protein L2|Ribosomal protein L2]]
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*[[Ribosomal protein L21|Ribosomal protein L21]]
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*[[Ribosomal protein L3|Ribosomal protein L3]]
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*[[Ribosomal protein L34|Ribosomal protein L34]]
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*[[Ribosomal protein L4|Ribosomal protein L4]]
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*[[Ribosomal protein L5|Ribosomal protein L5]]
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*[[Ribosomal protein L6|Ribosomal protein L6]]
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*[[Ribosomal protein L7|Ribosomal protein L7]]
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*[[Ribosome|Ribosome]]
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==Reference==
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<ref group="xtra">PMID:018455733</ref><references group="xtra"/>
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[[Category: Haloarcula marismortui]]
[[Category: Haloarcula marismortui]]
[[Category: Blaha, G.]]
[[Category: Blaha, G.]]

Revision as of 06:46, 14 May 2014

Structure of Anisomycin resistant 50S Ribosomal Subunit: 23S rRNA mutation C2487U

3cc7, resolution 2.70Å

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