1hht: Difference between revisions
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== | ==RNA dependent RNA polymerase from dsRNA bacteriophage phi6 plus template== | ||
In most RNA viruses, genome replication and transcription are catalysed by | <StructureSection load='1hht' size='340' side='right'caption='[[1hht]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1hht]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_virus_phi6 Pseudomonas virus phi6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HHT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HHT FirstGlance]. <br> | |||
</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></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=1hht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hht OCA], [https://pdbe.org/1hht PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hht RCSB], [https://www.ebi.ac.uk/pdbsum/1hht PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hht ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/RDRP_BPPH6 RDRP_BPPH6] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In most RNA viruses, genome replication and transcription are catalysed by a viral RNA-dependent RNA polymerase. Double-stranded RNA viruses perform these operations in a capsid (the polymerase complex), using an enzyme that can read both single- and double-stranded RNA. Structures have been solved for such viral capsids, but they do not resolve the polymerase subunits in any detail. Here we show that the 2 A resolution X-ray structure of the active polymerase subunit from the double-stranded RNA bacteriophage straight phi6 is highly similar to that of the polymerase of hepatitis C virus, providing an evolutionary link between double-stranded RNA viruses and flaviviruses. By crystal soaking and co-crystallization, we determined a number of other structures, including complexes with oligonucleotide and/or nucleoside triphosphates (NTPs), that suggest a mechanism by which the incoming double-stranded RNA is opened up to feed the template through to the active site, while the substrates enter by another route. The template strand initially overshoots, locking into a specificity pocket, and then, in the presence of cognate NTPs, reverses to form the initiation complex; this process engages two NTPs, one of which acts with the carboxy-terminal domain of the protein to prime the reaction. Our results provide a working model for the initiation of replication and transcription. | |||
A mechanism for initiating RNA-dependent RNA polymerization.,Butcher SJ, Grimes JM, Makeyev EV, Bamford DH, Stuart DI Nature. 2001 Mar 8;410(6825):235-40. PMID:11242087<ref>PMID:11242087</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1hht" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[RNA polymerase 3D structures|RNA polymerase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pseudomonas virus phi6]] | |||
[[Category: Bamford DH]] | |||
[[Category: Butcher SJ]] | |||
[[Category: Grimes JM]] | |||
[[Category: Makeyev EV]] | |||
[[Category: Stuart DI]] | |||