View source for 2jlf


==STRUCTURAL EXPLANATION FOR THE ROLE OF MN IN THE ACTIVITY OF PHI6 RNA- DEPENDENT RNA POLYMERASE==
<StructureSection load='2jlf' size='340' side='right'caption='[[2jlf]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2jlf]] 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=2JLF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JLF 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]] 3.2&#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=2jlf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jlf OCA], [https://pdbe.org/2jlf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jlf RCSB], [https://www.ebi.ac.uk/pdbsum/2jlf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jlf 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2jlf" 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: Poranen MM]]
[[Category: Salgado PS]]
[[Category: Stuart DI]]
[[Category: Wright S]]