1uvl: Difference between revisions
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< | ==The structural basis for RNA specificity and Ca2 inhibition of an RNA-dependent RNA polymerase phi6p2 with 5nt RNA. Conformation B== | ||
<StructureSection load='1uvl' size='340' side='right'caption='[[1uvl]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1uvl]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_virus_phi6 Pseudomonas virus phi6] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UVL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UVL 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]] 2Å</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=1uvl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uvl OCA], [https://pdbe.org/1uvl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uvl RCSB], [https://www.ebi.ac.uk/pdbsum/1uvl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uvl 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 RNA-dependent RNA polymerase of bacteriophage phi6 transcribes mRNA from the three segments of the dsRNA viral genome. We have cocrystallized RNA oligonucleotides with the polymerase, revealing the mode of binding of RNA templates. This binding is somewhat different from that previously seen for DNA oligomers, leading to additional RNA-protein hydrogen bonds, consistent with a preference for RNA. Activation of the RNA/polymerase complex by the addition of substrate and Mg2+ initiates a single round of reaction within the crystal to form a dead-end complex that partially collapses within the enzyme active site. By replacing Mg2+ with Ca2+, we have been able to capture the inhibited complex which shows distortion that explains the structural basis for the inhibition of such polymerases by Ca2+. | |||
The structural basis for RNA specificity and Ca2+ inhibition of an RNA-dependent RNA polymerase.,Salgado PS, Makeyev EV, Butcher SJ, Bamford DH, Stuart DI, Grimes JM Structure. 2004 Feb;12(2):307-16. PMID:14962391<ref>PMID:14962391</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1uvl" 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: Synthetic construct]] | |||
== | [[Category: Bamford D]] | ||
[[Category: Butcher S]] | |||
[[Category: | [[Category: Grimes JM]] | ||
[[Category: | [[Category: Makeyev EV]] | ||
[[Category: | [[Category: Salgado PS]] | ||
[[Category: | [[Category: Stuart DI]] | ||
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Latest revision as of 16:00, 13 December 2023
The structural basis for RNA specificity and Ca2 inhibition of an RNA-dependent RNA polymerase phi6p2 with 5nt RNA. Conformation BThe structural basis for RNA specificity and Ca2 inhibition of an RNA-dependent RNA polymerase phi6p2 with 5nt RNA. Conformation B
Structural highlights
FunctionPublication Abstract from PubMedThe RNA-dependent RNA polymerase of bacteriophage phi6 transcribes mRNA from the three segments of the dsRNA viral genome. We have cocrystallized RNA oligonucleotides with the polymerase, revealing the mode of binding of RNA templates. This binding is somewhat different from that previously seen for DNA oligomers, leading to additional RNA-protein hydrogen bonds, consistent with a preference for RNA. Activation of the RNA/polymerase complex by the addition of substrate and Mg2+ initiates a single round of reaction within the crystal to form a dead-end complex that partially collapses within the enzyme active site. By replacing Mg2+ with Ca2+, we have been able to capture the inhibited complex which shows distortion that explains the structural basis for the inhibition of such polymerases by Ca2+. The structural basis for RNA specificity and Ca2+ inhibition of an RNA-dependent RNA polymerase.,Salgado PS, Makeyev EV, Butcher SJ, Bamford DH, Stuart DI, Grimes JM Structure. 2004 Feb;12(2):307-16. PMID:14962391[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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