1nwy

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[[Image:1nwy.gif|left|200px]]
 
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{{Structure
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==COMPLEX OF THE LARGE RIBOSOMAL SUBUNIT FROM DEINOCOCCUS RADIODURANS WITH AZITHROMYCIN==
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|PDB= 1nwy |SIZE=350|CAPTION= <scene name='initialview01'>1nwy</scene>, resolution 3.30&Aring;
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<StructureSection load='1nwy' size='340' side='right'caption='[[1nwy]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=A:ADENOSINE-5&#39;-MONOPHOSPHATE'>A</scene>, <scene name='pdbligand=C:CYTIDINE-5&#39;-MONOPHOSPHATE'>C</scene>, <scene name='pdbligand=G:GUANOSINE-5&#39;-MONOPHOSPHATE'>G</scene>, <scene name='pdbligand=U:URIDINE-5&#39;-MONOPHOSPHATE'>U</scene>, <scene name='pdbligand=ZIT:AZITHROMYCIN'>ZIT</scene>
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<table><tr><td colspan='2'>[[1nwy]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NWY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NWY FirstGlance]. <br>
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|ACTIVITY=
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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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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZIT:AZITHROMYCIN'>ZIT</scene></td></tr>
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|DOMAIN=
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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=1nwy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nwy OCA], [https://pdbe.org/1nwy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nwy RCSB], [https://www.ebi.ac.uk/pdbsum/1nwy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nwy ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nwy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nwy OCA], [http://www.ebi.ac.uk/pdbsum/1nwy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nwy RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/RL23_DEIRA RL23_DEIRA] One of the early assembly protein (By similarity) it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. Forms the main docking site for trigger factor binding to the ribosome (PubMed:16091460 and PubMed:16271892).[HAMAP-Rule:MF_01369]
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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/nw/1nwy_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=1nwy 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 azalide azithromycin and the ketolide ABT-773, which were derived by chemical modifications of erythromycin, exhibit elevated activity against a number of penicillin- and macrolide-resistant pathogenic bacteria. Analysis of the crystal structures of the large ribosomal subunit from Deinococcus radiodurans complexed with azithromycin or ABT-773 indicates that, despite differences in the number and nature of their contacts with the ribosome, both compounds exert their antimicrobial activity by blocking the protein exit tunnel. In contrast to all macrolides studied so far, two molecules of azithromycin bind simultaneously to the tunnel. The additional molecule also interacts with two proteins, L4 and L22, implicated in macrolide resistance. These studies illuminated and rationalized the enhanced activity of the drugs against specific macrolide-resistant bacteria.
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'''COMPLEX OF THE LARGE RIBOSOMAL SUBUNIT FROM DEINOCOCCUS RADIODURANS WITH AZITHROMYCIN'''
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Structural basis for the antibiotic activity of ketolides and azalides.,Schlunzen F, Harms JM, Franceschi F, Hansen HA, Bartels H, Zarivach R, Yonath A Structure. 2003 Mar;11(3):329-38. PMID:12623020<ref>PMID:12623020</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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</div>
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<div class="pdbe-citations 1nwy" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The azalide azithromycin and the ketolide ABT-773, which were derived by chemical modifications of erythromycin, exhibit elevated activity against a number of penicillin- and macrolide-resistant pathogenic bacteria. Analysis of the crystal structures of the large ribosomal subunit from Deinococcus radiodurans complexed with azithromycin or ABT-773 indicates that, despite differences in the number and nature of their contacts with the ribosome, both compounds exert their antimicrobial activity by blocking the protein exit tunnel. In contrast to all macrolides studied so far, two molecules of azithromycin bind simultaneously to the tunnel. The additional molecule also interacts with two proteins, L4 and L22, implicated in macrolide resistance. These studies illuminated and rationalized the enhanced activity of the drugs against specific macrolide-resistant bacteria.
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*[[Ribosome 3D structures|Ribosome 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1NWY is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NWY OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Structural basis for the antibiotic activity of ketolides and azalides., Schlunzen F, Harms JM, Franceschi F, Hansen HA, Bartels H, Zarivach R, Yonath A, Structure. 2003 Mar;11(3):329-38. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12623020 12623020]
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[[Category: Deinococcus radiodurans]]
[[Category: Deinococcus radiodurans]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Bartels, H.]]
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[[Category: Bartels H]]
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[[Category: Franceschi, F.]]
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[[Category: Franceschi F]]
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[[Category: Hansen, H A.S.]]
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[[Category: Hansen HAS]]
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[[Category: Harms, J.]]
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[[Category: Harms J]]
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[[Category: Schluenzen, F.]]
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[[Category: Schluenzen F]]
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[[Category: Yonath, A.]]
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[[Category: Yonath A]]
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[[Category: Zarivach, R.]]
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[[Category: Zarivach R]]
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[[Category: 50]]
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[[Category: azithromycin]]
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[[Category: ketolide]]
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[[Category: macrolide]]
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[[Category: ribosomal]]
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[[Category: ribosome]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:36:41 2008''
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Current revision

COMPLEX OF THE LARGE RIBOSOMAL SUBUNIT FROM DEINOCOCCUS RADIODURANS WITH AZITHROMYCIN

PDB ID 1nwy

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