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1s0v

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Revision as of 07:06, 8 March 2018

Structural basis for substrate selection by T7 RNA polymerase

Structural highlights

1s0v is a 16 chain structure with sequence from Bpt7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1h38
Gene:	1 (BPT7)
Activity:	DNA-directed RNA polymerase, with EC number 2.7.7.6
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

[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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The mechanism by which nucleotide polymerases select the correct substrate is of fundamental importance to the fidelity of DNA replication and transcription. During the nucleotide addition cycle, pol I DNA polymerases undergo the transition from a catalytically inactive "open" to an active "closed" conformation. All known determinants of substrate selection are associated with the "closed" state. To elucidate if this mechanism is conserved in homologous single subunit RNA polymerases (RNAPs), we have determined the structure of T7 RNAP elongation complex with the incoming substrate analog. Surprisingly, the substrate specifically binds to RNAP in the "open" conformation, where it is base paired with the acceptor template base, while Tyr639 provides discrimination of ribose versus deoxyribose substrates. The structure therefore suggests a novel mechanism, in which the substrate selection occurs prior to the isomerization to the catalytically active conformation. Modeling of multisubunit RNAPs suggests that this mechanism might be universal for all RNAPs.

Structural basis for substrate selection by t7 RNA polymerase.,Temiakov D, Patlan V, Anikin M, McAllister WT, Yokoyama S, Vassylyev DG Cell. 2004 Feb 6;116(3):381-91. PMID:15016373^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Temiakov D, Patlan V, Anikin M, McAllister WT, Yokoyama S, Vassylyev DG. Structural basis for substrate selection by t7 RNA polymerase. Cell. 2004 Feb 6;116(3):381-91. PMID:15016373

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1s0v"

@@ Line 1: / Line 1: @@
 ==Structural basis for substrate selection by T7 RNA polymerase==
 <StructureSection load='1s0v' size='340' side='right' caption='[[1s0v]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10760 BPT7])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1s0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s0v OCA], [http://pdbe.org/1s0v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1s0v RCSB], [http://www.ebi.ac.uk/pdbsum/1s0v PDBsum], [http://www.topsan.org/Proteins/RSGI/1s0v TOPSAN]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1s0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s0v OCA], [http://pdbe.org/1s0v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1s0v RCSB], [http://www.ebi.ac.uk/pdbsum/1s0v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1s0v ProSAT], [http://www.topsan.org/Proteins/RSGI/1s0v TOPSAN]</span></td></tr>
 </table>
 == Function ==
@@ Line 15: / Line 16: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/s0/1s0v_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/s0/1s0v_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1s0v

From Proteopedia

Revision as of 07:06, 8 March 2018

Structural basis for substrate selection by T7 RNA polymerase

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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