3ccr: Difference between revisions

Revision as of 12:57, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:3ccr.png

Template:STRUCTURE 3ccr

Structure of Anisomycin resistant 50S Ribosomal Subunit: 23S rRNA mutation A2488C. Density for anisomycin is visible but not included in the model.Structure of Anisomycin resistant 50S Ribosomal Subunit: 23S rRNA mutation A2488C. Density for anisomycin is visible but not included in the model.

Template:ABSTRACT PUBMED 18455733

About this StructureAbout this Structure

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

ReferenceReference

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

Page seeded by OCA on Sun Jul 27 12:57:28 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:3ccr.jpg|left|200px]]
+{{Seed}}
+[[Image:3ccr.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_3ccr|  PDB=3ccr  |  SCENE=  }}
-'''Structure of Anisomycin resistant 50S Ribosomal Subunit: 23S rRNA mutation A2488C. Density for anisomycin is visible but not included in the model.'''
+===Structure of Anisomycin resistant 50S Ribosomal Subunit: 23S rRNA mutation A2488C. Density for anisomycin is visible but not included in the model.===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_18455733}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18455733 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18455733}}
 ==About this Structure==
@@ Line 28: / Line 32: @@
 [[Category: Large ribosomal subunit]]
 [[Category: Ribosome]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu May 22 22:00:24 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 12:57:28 2008''