4b02: Difference between revisions
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<StructureSection load='4b02' size='340' side='right'caption='[[4b02]], [[Resolution|resolution]] 3.30Å' scene=''> | <StructureSection load='4b02' size='340' side='right'caption='[[4b02]], [[Resolution|resolution]] 3.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4b02]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[4b02]] is a 3 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=4B02 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B02 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]] 3.3Å</td></tr> | ||
<tr id=' | <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=4b02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b02 OCA], [https://pdbe.org/4b02 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b02 RCSB], [https://www.ebi.ac.uk/pdbsum/4b02 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b02 ProSAT]</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=4b02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b02 OCA], [https://pdbe.org/4b02 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b02 RCSB], [https://www.ebi.ac.uk/pdbsum/4b02 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b02 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/RDRP_BPPH6 RDRP_BPPH6] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Pseudomonas virus phi6]] | ||
[[Category: Bamford | [[Category: Bamford DH]] | ||
[[Category: Chen | [[Category: Chen Q]] | ||
[[Category: Degerth | [[Category: Degerth LH]] | ||
[[Category: Grimes | [[Category: Grimes JM]] | ||
[[Category: Poranen | [[Category: Poranen MM]] | ||
[[Category: Sarin | [[Category: Sarin LP]] | ||
[[Category: Stuart | [[Category: Stuart DI]] | ||
[[Category: Wright | [[Category: Wright S]] | ||
Latest revision as of 14:39, 20 December 2023
The C-terminal Priming Domain is Strongly Associated with the Main Body of Bacteriophage phi6 RNA-Dependent RNA PolymeraseThe C-terminal Priming Domain is Strongly Associated with the Main Body of Bacteriophage phi6 RNA-Dependent RNA Polymerase
Structural highlights
FunctionPublication Abstract from PubMedDouble-stranded RNA viruses encode a single protein species containing RNA-dependent RNA polymerase (RdRP) motifs. This protein is responsible for RNA transcription and replication. The architecture of viral RdRPs resembles that of a cupped right hand with fingers, palm and thumb domains. Those using de novo initiation have a flexible structural elaboration that constitutes the priming platform. Here we investigate the properties of the C-terminal priming domain of bacteriophage varphi6 to get insights into the role of an extended loop connecting this domain to the main body of the polymerase. Proteolyzed varphi6 RdRP that possesses a nick in the hinge region of this loop was better suited for de novo initiation. The clipped C-terminus remained associated with the main body of the polymerase via the anchor helix. The structurally flexible hinge region appeared to be involved in the control of priming platform movement. Moreover, we detected abortive initiation products for a bacteriophage RdRP. The C-terminal priming domain is strongly associated with the main body of bacteriophage varphi6 RNA-dependent RNA polymerase.,Sarin LP, Wright S, Chen Q, Degerth LH, Stuart DI, Grimes JM, Bamford DH, Poranen MM Virology. 2012 Oct 10;432(1):184-93. Epub 2012 Jul 6. PMID:22770923[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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