2jl9: Difference between revisions
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==Structural explanation for the role of Mn in the activity of phi6 RNA- dependent RNA polymerase== | |||
<StructureSection load='2jl9' size='340' side='right' caption='[[2jl9]], [[Resolution|resolution]] 3.20Å' scene=''> | <StructureSection load='2jl9' size='340' side='right' caption='[[2jl9]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1uvn|1uvn]], [[1uvj|1uvj]], [[1hht|1hht]], [[1hi1|1hi1]], [[1wac|1wac]], [[1uvm|1uvm]], [[1uvk|1uvk]], [[1hhs|1hhs]], [[1hi0|1hi0]], [[1uvi|1uvi]], [[1uvl|1uvl]], [[1hi8|1hi8]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1uvn|1uvn]], [[1uvj|1uvj]], [[1hht|1hht]], [[1hi1|1hi1]], [[1wac|1wac]], [[1uvm|1uvm]], [[1uvk|1uvk]], [[1hhs|1hhs]], [[1hi0|1hi0]], [[1uvi|1uvi]], [[1uvl|1uvl]], [[1hi8|1hi8]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RNA-directed_RNA_polymerase RNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.48 2.7.7.48] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RNA-directed_RNA_polymerase RNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.48 2.7.7.48] </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=2jl9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jl9 OCA], [http://pdbe.org/2jl9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jl9 RCSB], [http://www.ebi.ac.uk/pdbsum/2jl9 PDBsum]</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=2jl9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jl9 OCA], [http://pdbe.org/2jl9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jl9 RCSB], [http://www.ebi.ac.uk/pdbsum/2jl9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2jl9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Revision as of 10:08, 11 July 2018
Structural explanation for the role of Mn in the activity of phi6 RNA- dependent RNA polymeraseStructural explanation for the role of Mn in the activity of phi6 RNA- dependent RNA polymerase
Structural highlights
Publication Abstract from PubMedThe biological role of manganese (Mn(2+)) has been a long-standing puzzle, since at low concentrations it activates several polymerases whilst at higher concentrations it inhibits. Viral RNA polymerases possess a common architecture, reminiscent of a closed right hand. The RNA-dependent RNA polymerase (RdRp) of bacteriophage 6 is one of the best understood examples of this important class of polymerases. We have probed the role of Mn(2+) by biochemical, biophysical and structural analyses of the wild-type enzyme and of a mutant form with an altered Mn(2+)-binding site (E491 to Q). The E491Q mutant has much reduced affinity for Mn(2+), reduced RNA binding and a compromised elongation rate. Loss of Mn(2+) binding structurally stabilizes the enzyme. These data and a re-examination of the structures of other viral RNA polymerases clarify the role of manganese in the activation of polymerization: Mn(2+) coordination of a catalytic aspartate is necessary to allow the active site to properly engage with the triphosphates of the incoming NTPs. The structural flexibility caused by Mn(2+) is also important for the enzyme dynamics, explaining the requirement for manganese throughout RNA polymerization. Structural explanation for the role of Mn2+ in the activity of {phi}6 RNA-dependent RNA polymerase.,Poranen MM, Salgado PS, Koivunen MR, Wright S, Bamford DH, Stuart DI, Grimes JM Nucleic Acids Res. 2008 Oct 21. PMID:18940872[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Bpph6
- RNA-directed RNA polymerase
- Bamford, D H
- Grimes, J M
- Koivunen, M R.L
- Poranen, M M
- Salgado, P S
- Stuart, D I
- Wright, S
- Magnesium
- Manganese
- Metal-binding
- Nucleotide-binding
- Nucleotidyltransferase
- Oligonucleotide
- Polymerase
- Polymerase-complex
- Rna replication
- Rna-dependent rna polymerase
- Rna-directed rna polymerase
- Transferase
- Virion