3cc4: Difference between revisions

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[[Image:3cc4.jpg|left|200px]]
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{{STRUCTURE_3cc4|  PDB=3cc4  |  SCENE=  }}  
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'''Co-crystal Structure of Anisomycin Bound to the 50S Ribosomal Subunit'''
===Co-crystal Structure of Anisomycin Bound to the 50S Ribosomal Subunit===




==Overview==
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Eleven mutations that make Haloarcula marismortui resistant to anisomycin, an antibiotic that competes with the amino acid side chains of aminoacyl tRNAs for binding to the A-site cleft of the large ribosomal unit, have been identified in 23S rRNA. The correlation observed between the sensitivity of H. marismortui to anisomycin and the affinity of its large ribosomal subunits for the drug indicates that its response to anisomycin is determined primarily by the binding of the drug to its large ribosomal subunit. The structures of large ribosomal subunits containing resistance mutations show that these mutations can be divided into two classes: (1) those that interfere with specific drug-ribosome interactions and (2) those that stabilize the apo conformation of the A-site cleft of the ribosome relative to its drug-bound conformation. The conformational effects of some mutations of the second kind propagate through the ribosome for considerable distances and are reversed when A-site substrates bind to the ribosome.
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{{ABSTRACT_PUBMED_18455733}}


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Mutations outside the anisomycin-binding site can make ribosomes drug-resistant., Blaha G, Gurel G, Schroeder SJ, Moore PB, Steitz TA, J Mol Biol. 2008 Jun 6;379(3):505-19. Epub 2008 Apr 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18455733 18455733]
Mutations outside the anisomycin-binding site can make ribosomes drug-resistant., Blaha G, Gurel G, Schroeder SJ, Moore PB, Steitz TA, J Mol Biol. 2008 Jun 6;379(3):505-19. Epub 2008 Apr 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18455733 18455733]
Structures of five antibiotics bound at the peptidyl transferase center of the large ribosomal subunit., Hansen JL, Moore PB, Steitz TA, J Mol Biol. 2003 Jul 25;330(5):1061-75. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12860128 12860128]
[[Category: Haloarcula marismortui]]
[[Category: Haloarcula marismortui]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Ribosome]]
[[Category: Ribosome]]
[[Category: Wild type]]
[[Category: Wild type]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu May 22 21:58:39 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:20:08 2008''

Revision as of 17:20, 28 July 2008

File:3cc4.png

Template:STRUCTURE 3cc4

Co-crystal Structure of Anisomycin Bound to the 50S Ribosomal Subunit

Template:ABSTRACT PUBMED 18455733

About this Structure

3CC4 is a Protein complex structure of sequences from Haloarcula marismortui. Full crystallographic information is available from OCA.

Reference

Mutations outside the anisomycin-binding site can make ribosomes drug-resistant., Blaha G, Gurel G, Schroeder SJ, Moore PB, Steitz TA, J Mol Biol. 2008 Jun 6;379(3):505-19. Epub 2008 Apr 8. PMID:18455733

Structures of five antibiotics bound at the peptidyl transferase center of the large ribosomal subunit., Hansen JL, Moore PB, Steitz TA, J Mol Biol. 2003 Jul 25;330(5):1061-75. PMID:12860128

Page seeded by OCA on Mon Jul 28 20:20:08 2008

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