1jzz: Difference between revisions
New page: left|200px<br /><applet load="1jzz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jzz, resolution 3.8Å" /> '''Structural Basis for ... |
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[[Image:1jzz.gif|left|200px]]<br /><applet load="1jzz" size=" | [[Image:1jzz.gif|left|200px]]<br /><applet load="1jzz" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1jzz, resolution 3.8Å" /> | caption="1jzz, resolution 3.8Å" /> | ||
'''Structural Basis for the Interaction of Antibiotics with the Peptidyl Transferase Center in Eubacteria'''<br /> | '''Structural Basis for the Interaction of Antibiotics with the Peptidyl Transferase Center in Eubacteria'''<br /> | ||
==Overview== | ==Overview== | ||
Ribosomes, the site of protein synthesis, are a major target for natural | Ribosomes, the site of protein synthesis, are a major target for natural and synthetic antibiotics. Detailed knowledge of antibiotic binding sites is central to understanding the mechanisms of drug action. Conversely, drugs are excellent tools for studying the ribosome function. To elucidate the structural basis of ribosome-antibiotic interactions, we determined the high-resolution X-ray structures of the 50S ribosomal subunit of the eubacterium Deinococcus radiodurans, complexed with the clinically relevant antibiotics chloramphenicol, clindamycin and the three macrolides erythromycin, clarithromycin and roxithromycin. We found that antibiotic binding sites are composed exclusively of segments of 23S ribosomal RNA at the peptidyl transferase cavity and do not involve any interaction of the drugs with ribosomal proteins. Here we report the details of antibiotic interactions with the components of their binding sites. Our results also show the importance of putative Mg+2 ions for the binding of some drugs. This structural analysis should facilitate rational drug design. | ||
==About this Structure== | ==About this Structure== | ||
1JZZ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans] with ROX and MG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1JZZ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans] with <scene name='pdbligand=ROX:'>ROX</scene> and <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JZZ OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: roxithromycin]] | [[Category: roxithromycin]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:28:34 2008'' | ||
Revision as of 14:28, 21 February 2008
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Structural Basis for the Interaction of Antibiotics with the Peptidyl Transferase Center in Eubacteria
OverviewOverview
Ribosomes, the site of protein synthesis, are a major target for natural and synthetic antibiotics. Detailed knowledge of antibiotic binding sites is central to understanding the mechanisms of drug action. Conversely, drugs are excellent tools for studying the ribosome function. To elucidate the structural basis of ribosome-antibiotic interactions, we determined the high-resolution X-ray structures of the 50S ribosomal subunit of the eubacterium Deinococcus radiodurans, complexed with the clinically relevant antibiotics chloramphenicol, clindamycin and the three macrolides erythromycin, clarithromycin and roxithromycin. We found that antibiotic binding sites are composed exclusively of segments of 23S ribosomal RNA at the peptidyl transferase cavity and do not involve any interaction of the drugs with ribosomal proteins. Here we report the details of antibiotic interactions with the components of their binding sites. Our results also show the importance of putative Mg+2 ions for the binding of some drugs. This structural analysis should facilitate rational drug design.
About this StructureAbout this Structure
1JZZ is a Protein complex structure of sequences from Deinococcus radiodurans with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria., Schlunzen F, Zarivach R, Harms J, Bashan A, Tocilj A, Albrecht R, Yonath A, Franceschi F, Nature. 2001 Oct 25;413(6858):814-21. PMID:11677599
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