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[[Image:1nwx.gif|left|200px]]
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{{STRUCTURE_1nwx|  PDB=1nwx  |  SCENE=  }}
'''COMPLEX OF THE LARGE RIBOSOMAL SUBUNIT FROM DEINOCOCCUS RADIODURANS WITH ABT-773'''


==COMPLEX OF THE LARGE RIBOSOMAL SUBUNIT FROM DEINOCOCCUS RADIODURANS WITH ABT-773==
<StructureSection load='1nwx' size='340' side='right'caption='[[1nwx]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1nwx]] 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=1NWX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NWX 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]] 3.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=773:CETHROMYCIN'>773</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=1nwx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nwx OCA], [https://pdbe.org/1nwx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nwx RCSB], [https://www.ebi.ac.uk/pdbsum/1nwx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nwx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RL9_DEIRA RL9_DEIRA] Binds to the 23S rRNA and protein L31.[HAMAP-Rule:MF_00503]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nw/1nwx_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1nwx ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1NWX 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=1NWX OCA].
</div>
<div class="pdbe-citations 1nwx" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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]
*[[Ribosome 3D structures|Ribosome 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Deinococcus radiodurans]]
[[Category: Deinococcus radiodurans]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Bartels, H.]]
[[Category: Bartels H]]
[[Category: Franceschi, F.]]
[[Category: Franceschi F]]
[[Category: Hansen, H A.S.]]
[[Category: Hansen HAS]]
[[Category: Harms, J.]]
[[Category: Harms J]]
[[Category: Schluenzen, F.]]
[[Category: Schluenzen F]]
[[Category: Yonath, A.]]
[[Category: Yonath A]]
[[Category: Zarivach, R.]]
[[Category: Zarivach R]]
[[Category: 50]]
[[Category: Abt-773]]
[[Category: Ketolide]]
[[Category: Macrolide]]
[[Category: Ribosomal subunit]]
[[Category: Ribosome]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 03:04:40 2008''