2a6e: Difference between revisions

Revision as of 19:55, 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:2a6e.png

Template:STRUCTURE 2a6e

Crystal structure of the T. Thermophilus RNA polymerase holoenzymeCrystal structure of the T. Thermophilus RNA polymerase holoenzyme

Template:ABSTRACT PUBMED 16096056

About this StructureAbout this Structure

2A6E is a Protein complex structure of sequences from Thermus thermophilus. Full crystallographic information is available from OCA.

ReferenceReference

Allosteric modulation of the RNA polymerase catalytic reaction is an essential component of transcription control by rifamycins., Artsimovitch I, Vassylyeva MN, Svetlov D, Svetlov V, Perederina A, Igarashi N, Matsugaki N, Wakatsuki S, Tahirov TH, Vassylyev DG, Cell. 2005 Aug 12;122(3):351-63. PMID:16096056

Page seeded by OCA on Sun Jul 27 19:55:47 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:2a6e.gif|left|200px]]
+{{Seed}}
+[[Image:2a6e.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2a6e|  PDB=2a6e  |  SCENE=  }}
-'''Crystal structure of the T. Thermophilus RNA polymerase holoenzyme'''
+===Crystal structure of the T. Thermophilus RNA polymerase holoenzyme===
-==Overview==
+<!--
-Rifamycins, the clinically important antibiotics, target bacterial RNA polymerase (RNAP). A proposed mechanism in which rifamycins sterically block the extension of nascent RNA beyond three nucleotides does not alone explain why certain RNAP mutations confer resistance to some but not other rifamycins. Here we show that unlike rifampicin and rifapentin, and contradictory to the steric model, rifabutin inhibits formation of the first and second phosphodiester bonds. We report 2.5 A resolution structures of rifabutin and rifapentin complexed with the Thermus thermophilus RNAP holoenzyme. The structures reveal functionally important distinct interactions of antibiotics with the initiation sigma factor. Strikingly, both complexes lack the catalytic Mg2+ ion observed in the apo-holoenzyme, whereas an increase in Mg2+ concentration confers resistance to rifamycins. We propose that a rifamycin-induced signal is transmitted over approximately 19 A to the RNAP active site to slow down catalysis. Based on structural predictions, we designed enzyme substitutions that apparently interrupt this allosteric signal.
+The line below this paragraph, {{ABSTRACT_PUBMED_16096056}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16096056 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16096056}}
 ==About this Structure==
@@ Line 40: / Line 44: @@
 [[Category: Structural genomic]]
 [[Category: Transcription regulation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 18:40:00 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:55:47 2008''