2o5i
From Proteopedia
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| - | [[Image:2o5i.gif|left|200px]] | + | [[Image:2o5i.gif|left|200px]] |
| - | + | ||
| - | '''Crystal structure of the T. thermophilus RNA polymerase elongation complex''' | + | {{Structure |
| + | |PDB= 2o5i |SIZE=350|CAPTION= <scene name='initialview01'>2o5i</scene>, resolution 2.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/DNA-directed_RNA_polymerase DNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.6 2.7.7.6] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of the T. thermophilus RNA polymerase elongation complex''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2O5I is a [ | + | 2O5I is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O5I OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17581590 17581590] |
[[Category: DNA-directed RNA polymerase]] | [[Category: DNA-directed RNA polymerase]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: template dna]] | [[Category: template dna]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:55:21 2008'' |
Revision as of 15:55, 20 March 2008
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| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | DNA-directed RNA polymerase, with EC number 2.7.7.6 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the T. thermophilus RNA polymerase elongation complex
Overview
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.
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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