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1cez

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|PDB= 1cez |SIZE=350|CAPTION= <scene name='initialview01'>1cez</scene>, resolution 2.40&Aring;
|PDB= 1cez |SIZE=350|CAPTION= <scene name='initialview01'>1cez</scene>, resolution 2.40&Aring;
|SITE=
|SITE=
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|LIGAND=
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|LIGAND= <scene name='pdbligand=DA:2&#39;-DEOXYADENOSINE-5&#39;-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2&#39;-DEOXYCYTIDINE-5&#39;-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2&#39;-DEOXYGUANOSINE-5&#39;-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5&#39;-MONOPHOSPHATE'>DT</scene>
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|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]
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|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=
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|DOMAIN=
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|RELATEDENTRY=
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|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==
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1CEZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t7 Bacteriophage t7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CEZ OCA].
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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]
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[[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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:23:35 2008''
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''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


PDB ID 1cez

Drag the structure with the mouse to rotate
, 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

Page seeded by OCA on Sun Mar 30 19:20:25 2008

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