2o5i

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[[Image:2o5i.gif|left|200px]]
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{{Seed}}
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{{STRUCTURE_2o5i| PDB=2o5i | SCENE= }}
{{STRUCTURE_2o5i| PDB=2o5i | SCENE= }}
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'''Crystal structure of the T. thermophilus RNA polymerase elongation complex'''
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===Crystal structure of the T. thermophilus RNA polymerase elongation complex===
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==Overview==
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The RNA polymerase elongation complex (EC) is both highly stable and processive, rapidly extending RNA chains for thousands of nucleotides. Understanding the mechanisms of elongation and its regulation requires detailed information about the structural organization of the EC. Here we report the 2.5-A resolution structure of the Thermus thermophilus EC; the structure reveals the post-translocated intermediate with the DNA template in the active site available for pairing with the substrate. DNA strand separation occurs one position downstream of the active site, implying that only one substrate at a time can specifically bind to the EC. The upstream edge of the RNA/DNA hybrid stacks on the beta'-subunit 'lid' loop, whereas the first displaced RNA base is trapped within a protein pocket, suggesting a mechanism for RNA displacement. The RNA is threaded through the RNA exit channel, where it adopts a conformation mimicking that of a single strand within a double helix, providing insight into a mechanism for hairpin-dependent pausing and termination.
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(as it appears on PubMed at http://www.pubmed.gov), where 17581590 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17581590}}
==About this Structure==
==About this Structure==
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[[Category: Rna transcript]]
[[Category: Rna transcript]]
[[Category: Template dna]]
[[Category: Template dna]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 10:21:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:03:55 2008''

Revision as of 04:04, 29 July 2008

Template:STRUCTURE 2o5i

Crystal structure of the T. thermophilus RNA polymerase elongation complex

Template:ABSTRACT PUBMED 17581590

About this Structure

2O5I is a Protein complex structure of sequences from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

Structural basis for transcription elongation by bacterial RNA polymerase., Vassylyev DG, Vassylyeva MN, Perederina A, Tahirov TH, Artsimovitch I, Nature. 2007 Jul 12;448(7150):157-62. Epub 2007 Jun 20. PMID:17581590

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