1nwy
From Proteopedia
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|PDB= 1nwy |SIZE=350|CAPTION= <scene name='initialview01'>1nwy</scene>, resolution 3.30Å | |PDB= 1nwy |SIZE=350|CAPTION= <scene name='initialview01'>1nwy</scene>, resolution 3.30Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZIT:AZITHROMYCIN'>ZIT</scene> | + | |LIGAND= <scene name='pdbligand=A:ADENOSINE-5'-MONOPHOSPHATE'>A</scene>, <scene name='pdbligand=C:CYTIDINE-5'-MONOPHOSPHATE'>C</scene>, <scene name='pdbligand=G:GUANOSINE-5'-MONOPHOSPHATE'>G</scene>, <scene name='pdbligand=U:URIDINE-5'-MONOPHOSPHATE'>U</scene>, <scene name='pdbligand=ZIT:AZITHROMYCIN'>ZIT</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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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[[Category: Yonath, A.]] | [[Category: Yonath, A.]] | ||
[[Category: Zarivach, R.]] | [[Category: Zarivach, R.]] | ||
| - | [[Category: ZIT]] | ||
[[Category: 50]] | [[Category: 50]] | ||
[[Category: azithromycin]] | [[Category: azithromycin]] | ||
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[[Category: ribosome]] | [[Category: ribosome]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:36:41 2008'' |
Revision as of 19:36, 30 March 2008
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| , resolution 3.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
COMPLEX OF THE LARGE RIBOSOMAL SUBUNIT FROM DEINOCOCCUS RADIODURANS WITH AZITHROMYCIN
Overview
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
1NWY is a Protein complex structure of sequences from Deinococcus radiodurans. Full crystallographic information is available from OCA.
Reference
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
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