1hi8
From Proteopedia
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| - | [[ | + | ==RNA DEPENDENT RNA POLYMERASE FROM DSRNA BACTERIOPHAGE PHI6== |
| + | <StructureSection load='1hi8' size='340' side='right' caption='[[1hi8]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1hi8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_phage_phi6 Pseudomonas phage phi6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HI8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HI8 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hhs|1hhs]], [[1hht|1hht]], [[1hi0|1hi0]], [[1hi1|1hi1]]</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=1hi8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hi8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1hi8 RCSB], [http://www.ebi.ac.uk/pdbsum/1hi8 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <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> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Pseudomonas phage phi6]] | [[Category: Pseudomonas phage phi6]] | ||
[[Category: Bamford, D H.]] | [[Category: Bamford, D H.]] | ||
Revision as of 11:34, 20 October 2014
RNA DEPENDENT RNA POLYMERASE FROM DSRNA BACTERIOPHAGE PHI6
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