1h38: Difference between revisions
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<StructureSection load='1h38' size='340' side='right'caption='[[1h38]], [[Resolution|resolution]] 2.90Å' scene=''> | <StructureSection load='1h38' size='340' side='right'caption='[[1h38]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1h38]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1h38]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_phage_T7 Escherichia phage T7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H38 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H38 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1h38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h38 OCA], [https://pdbe.org/1h38 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h38 RCSB], [https://www.ebi.ac.uk/pdbsum/1h38 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h38 ProSAT], [https://www.topsan.org/Proteins/RSGI/1h38 TOPSAN]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1h38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h38 OCA], [https://pdbe.org/1h38 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h38 RCSB], [https://www.ebi.ac.uk/pdbsum/1h38 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h38 ProSAT], [https://www.topsan.org/Proteins/RSGI/1h38 TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/RPOL_BPT7 RPOL_BPT7] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of the late genes of T7. It is rifampicin-resistant. It recognizes a specific promoter sequence, unwinds the double-stranded RNA to expose the coding strand for templating, initiates transcription preferentially with a purine. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia phage T7]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Anikin | [[Category: Anikin M]] | ||
[[Category: McAllister | [[Category: McAllister WT]] | ||
[[Category: Patlan | [[Category: Patlan V]] | ||
[[Category: Tahirov | [[Category: Tahirov TH]] | ||
[[Category: Temyakov | [[Category: Temyakov D]] | ||
[[Category: Vassylyev | [[Category: Vassylyev DG]] | ||
[[Category: Yokoyama | [[Category: Yokoyama S]] | ||
Latest revision as of 15:16, 13 December 2023
Structure of a T7 RNA polymerase elongation complex at 2.9A resolutionStructure of a T7 RNA polymerase elongation complex at 2.9A resolution
Structural highlights
FunctionRPOL_BPT7 DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of the late genes of T7. It is rifampicin-resistant. It recognizes a specific promoter sequence, unwinds the double-stranded RNA to expose the coding strand for templating, initiates transcription preferentially with a purine. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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