1h38
From Proteopedia
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|PDB= 1h38 |SIZE=350|CAPTION= <scene name='initialview01'>1h38</scene>, resolution 2.90Å | |PDB= 1h38 |SIZE=350|CAPTION= <scene name='initialview01'>1h38</scene>, resolution 2.90Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=A:ADENOSINE-5'-MONOPHOSPHATE'>A</scene>, <scene name='pdbligand=C:CYTIDINE-5'-MONOPHOSPHATE'>C</scene>, <scene name='pdbligand=DA:2'-DEOXYADENOSINE-5'-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5'-MONOPHOSPHATE'>DT</scene>, <scene name='pdbligand=G:GUANOSINE-5'-MONOPHOSPHATE'>G</scene>, <scene name='pdbligand=U:URIDINE-5'-MONOPHOSPHATE'>U</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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h38 OCA], [http://www.ebi.ac.uk/pdbsum/1h38 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h38 RCSB]</span> | ||
}} | }} | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1H38 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ | + | 1H38 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t7 Enterobacteria phage t7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H38 OCA]. |
==Reference== | ==Reference== | ||
Structure of a T7 RNA polymerase elongation complex at 2.9 A resolution., Tahirov TH, Temiakov D, Anikin M, Patlan V, McAllister WT, Vassylyev DG, Yokoyama S, Nature. 2002 Nov 7;420(6911):43-50. Epub 2002 Oct 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12422209 12422209] | Structure of a T7 RNA polymerase elongation complex at 2.9 A resolution., Tahirov TH, Temiakov D, Anikin M, Patlan V, McAllister WT, Vassylyev DG, Yokoyama S, Nature. 2002 Nov 7;420(6911):43-50. Epub 2002 Oct 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12422209 12422209] | ||
| - | [[Category: Bacteriophage t7]] | ||
[[Category: DNA-directed RNA polymerase]] | [[Category: DNA-directed RNA polymerase]] | ||
| + | [[Category: Enterobacteria phage t7]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Anikin, M.]] | [[Category: Anikin, M.]] | ||
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[[Category: t7 rna polymerase]] | [[Category: t7 rna polymerase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:56:48 2008'' |
Revision as of 17:57, 30 March 2008
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| , resolution 2.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , , , , | ||||||
| Activity: | DNA-directed RNA polymerase, with EC number 2.7.7.6 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF A T7 RNA POLYMERASE ELONGATION COMPLEX AT 2.9A RESOLUTION
Overview
The single-subunit bacteriophage T7 RNA polymerase carries out the transcription cycle in an identical manner to that of bacterial and eukaryotic multisubunit enzymes. Here we report the crystal structure of a T7 RNA polymerase elongation complex, which shows that incorporation of an 8-base-pair RNA-DNA hybrid into the active site of the enzyme induces a marked rearrangement of the amino-terminal domain. This rearrangement involves alternative folding of about 130 residues and a marked reorientation (about 130 degrees rotation) of a stable core subdomain, resulting in a structure that provides elements required for stable transcription elongation. A wide opening on the enzyme surface that is probably an RNA exit pathway is formed, and the RNA-DNA hybrid is completely buried in a newly formed, deep protein cavity. Binding of 10 base pairs of downstream DNA is stabilized mostly by long-distance electrostatic interactions. The structure implies plausible mechanisms for the various phases of the transcription cycle, and reveals important structural similarities with the multisubunit RNA polymerases.
About this Structure
1H38 is a Protein complex structure of sequences from Enterobacteria phage t7. Full crystallographic information is available from OCA.
Reference
Structure of a T7 RNA polymerase elongation complex at 2.9 A resolution., Tahirov TH, Temiakov D, Anikin M, Patlan V, McAllister WT, Vassylyev DG, Yokoyama S, Nature. 2002 Nov 7;420(6911):43-50. Epub 2002 Oct 9. PMID:12422209
Page seeded by OCA on Sun Mar 30 20:56:48 2008
Categories: DNA-directed RNA polymerase | Enterobacteria phage t7 | Protein complex | Anikin, M. | Mcallister, W T. | Patlan, V. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Tahirov, T H. | Temyakov, D. | Vassylyev, D G. | Yokoyama, S. | Elongation complex | Protein/dna/rna | Riken structural genomics/proteomics initiative | Rsgi | Structural genomic | T7 rna polymerase
