1cez
From Proteopedia
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|PDB= 1cez |SIZE=350|CAPTION= <scene name='initialview01'>1cez</scene>, resolution 2.40Å | |PDB= 1cez |SIZE=350|CAPTION= <scene name='initialview01'>1cez</scene>, resolution 2.40Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <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> |
| - | |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=1cez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cez OCA], [http://www.ebi.ac.uk/pdbsum/1cez PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cez RCSB]</span> | ||
}} | }} | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CEZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | + | 1CEZ is a [[Single protein]] structure of sequence 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=1CEZ OCA]. |
==Reference== | ==Reference== | ||
Structural basis for initiation of transcription from an RNA polymerase-promoter complex., Cheetham GM, Jeruzalmi D, Steitz TA, Nature. 1999 May 6;399(6731):80-3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10331394 10331394] | Structural basis for initiation of transcription from an RNA polymerase-promoter complex., Cheetham GM, Jeruzalmi D, Steitz TA, Nature. 1999 May 6;399(6731):80-3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10331394 10331394] | ||
| - | [[Category: Bacteriophage t7]] | ||
[[Category: DNA-directed RNA polymerase]] | [[Category: DNA-directed RNA polymerase]] | ||
| + | [[Category: Enterobacteria phage t7]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Cheetham, G M.T.]] | [[Category: Cheetham, G M.T.]] | ||
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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 19:20:25 2008'' |
Revision as of 16:20, 30 March 2008
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| , resolution 2.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Activity: | DNA-directed RNA polymerase, with EC number 2.7.7.6 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF A T7 RNA POLYMERASE-T7 PROMOTER COMPLEX
Overview
Although the single-polypeptide-chain RNA polymerase from bacteriophage T7 (T7RNAP), like other RNA polymerases, uses the same mechanism of polymerization as the DNA polymerases, it can also recognize a specific promoter sequence, initiate new RNA chains from a single nucleotide, abortively cycle the synthesis of short transcripts, be regulated by a transcription inhibitor, and terminate transcription. As T7RNAP is homologous to the Pol I family of DNA polymerases, the differences between the structure of T7RNAP complexed to substrates and that of the corresponding DNA polymerase complex provides a structural basis for understanding many of these functional differences. T7RNAP initiates RNA synthesis at promoter sequences that are conserved from positions -17 to +6 relative to the start site of transcription. The crystal structure at 2.4 A resolution of T7RNAP complexed with a 17-base-pair promoter shows that the four base pairs closest to the catalytic active site have melted to form a transcription bubble. The T7 promoter sequence is recognized by interactions in the major groove between an antiparallel beta-loop and bases. The amino-terminal domain is involved in promoter recognition and DNA melting. We have also used homology modelling of the priming and incoming nucleoside triphosphates from the T7 DNA-polymerase ternary complex structure to explain the specificity of T7RNAP for ribonucleotides, its ability to initiate from a single nucleotide, and the abortive cycling at the initiation of transcription.
About this Structure
1CEZ is a Single protein structure of sequence from Enterobacteria phage t7. Full crystallographic information is available from OCA.
Reference
Structural basis for initiation of transcription from an RNA polymerase-promoter complex., Cheetham GM, Jeruzalmi D, Steitz TA, Nature. 1999 May 6;399(6731):80-3. PMID:10331394
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