1hht: Difference between revisions

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OCA

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-[[Image:1hht.gif|left|200px]]<br />
-<applet load="1hht" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1hht, resolution 2.9&Aring;" />
-'''RNA DEPENDENT RNA POLYMERASE FROM DSRNA BACTERIOPHAGE PHI6 PLUS TEMPLATE'''<br />
-==Overview==
+==RNA dependent RNA polymerase from dsRNA bacteriophage phi6 plus template==
-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 ... [[http://ispc.weizmann.ac.il/pmbin/getpm?11242087 (full description)]]
+<StructureSection load='1hht' size='340' side='right'caption='[[1hht]], [[Resolution|resolution]] 2.90&Aring;' 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]] 2.9&#8491;</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.
-==About this Structure==
+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>
-HHT is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacteriophage_phi-6 Bacteriophage phi-6]] with MN as [[http://en.wikipedia.org/wiki/ligand ligand]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HHT OCA]].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11242087 11242087]
+</div>
-[[Category: Bacteriophage phi-6]]
+<div class="pdbe-citations 1hht" style="background-color:#fffaf0;"></div>
-[[Category: Single protein]]
-[[Category: Bamford, D.H.]]
-[[Category: Butcher, S.J.]]
-[[Category: Grimes, J.M.]]
-[[Category: Makeyev, E.V.]]
-[[Category: Stuart, D.I.]]
-[[Category: MN]]
-[[Category: rna polymerase]]
-[[Category: viral polymerase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 18:42:35 2007''
+==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]]