1nwy

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(New page: 200px<br /><applet load="1nwy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nwy, resolution 3.30&Aring;" /> '''COMPLEX OF THE LARGE...)
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caption="1nwy, resolution 3.30&Aring;" />
'''COMPLEX OF THE LARGE RIBOSOMAL SUBUNIT FROM DEINOCOCCUS RADIODURANS WITH AZITHROMYCIN'''<br />
'''COMPLEX OF THE LARGE RIBOSOMAL SUBUNIT FROM DEINOCOCCUS RADIODURANS WITH AZITHROMYCIN'''<br />
==Overview==
==Overview==
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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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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==
==About this Structure==
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1NWY 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 ZIT as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NWY OCA].
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1NWY 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=ZIT:'>ZIT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NWY OCA].
==Reference==
==Reference==
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[[Category: Bartels, H.]]
[[Category: Bartels, H.]]
[[Category: Franceschi, F.]]
[[Category: Franceschi, F.]]
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[[Category: Hansen, H.A.S.]]
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[[Category: Hansen, H A.S.]]
[[Category: Harms, J.]]
[[Category: Harms, J.]]
[[Category: Schluenzen, F.]]
[[Category: Schluenzen, F.]]
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[[Category: ribosome]]
[[Category: ribosome]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:37:34 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:10:57 2008''

Revision as of 12:10, 21 February 2008

Image:1nwy.gif

1nwy, resolution 3.30Å

Drag the structure with the mouse to rotate

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 with as ligand. 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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