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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=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2jl9]] 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=2JL9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JL9 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]] 3.2Å</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=2jl9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jl9 OCA], [https://pdbe.org/2jl9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jl9 RCSB], [https://www.ebi.ac.uk/pdbsum/2jl9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jl9 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/RDRP_BPPH6 RDRP_BPPH6] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The 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<ref>PMID:18940872</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2jl9" 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: Grimes JM]] | ||
[[Category: Koivunen MRL]] | |||
[[Category: | [[Category: Poranen MM]] | ||
[[Category: | [[Category: Salgado PS]] | ||
[[Category: Bamford | [[Category: Stuart DI]] | ||
[[Category: Grimes | [[Category: Wright S]] | ||
[[Category: Koivunen | |||
[[Category: Poranen | |||
[[Category: Salgado | |||
[[Category: Stuart | |||
[[Category: Wright | |||
Latest revision as of 13:52, 25 October 2023
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
FunctionPublication 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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