1vp9

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<StructureSection load='1vp9' size='340' side='right'caption='[[1vp9]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
<StructureSection load='1vp9' size='340' side='right'caption='[[1vp9]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1vp9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vaccw Vaccw]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VP9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VP9 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1vp9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vaccinia_virus_WR Vaccinia virus WR]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VP9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VP9 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Polynucleotide_adenylyltransferase Polynucleotide adenylyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.19 2.7.7.19] </span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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=1vp9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vp9 OCA], [https://pdbe.org/1vp9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vp9 RCSB], [https://www.ebi.ac.uk/pdbsum/1vp9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vp9 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=1vp9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vp9 OCA], [https://pdbe.org/1vp9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vp9 RCSB], [https://www.ebi.ac.uk/pdbsum/1vp9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vp9 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/MCE_VACCW MCE_VACCW]] Displays methyltransferase, positive regulation of the poly(A) polymerase and transcription elongation activities. Involved in the modification of both mRNA ends and in intermediate and late gene positive transcription elongation. At the mRNAs 5' end, methylates the ribose 2' OH group of the first transcribed nucleotide, thereby producing a 2'-O-methylpurine cap. At the 3' end, functions as a processivity factor which stimulates the activity of the viral poly(A) polymerase VP55 that creates mRNA's poly(A) tail. In the presence of VP39, VP55 does not dissociate from the RNA allowing tail elongation to around 250 adenylates.<ref>PMID:1313572</ref> <ref>PMID:1670500</ref> <ref>PMID:12359447</ref>
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[https://www.uniprot.org/uniprot/MCE_VACCW MCE_VACCW] Displays methyltransferase, positive regulation of the poly(A) polymerase and transcription elongation activities. Involved in the modification of both mRNA ends and in intermediate and late gene positive transcription elongation. At the mRNAs 5' end, methylates the ribose 2' OH group of the first transcribed nucleotide, thereby producing a 2'-O-methylpurine cap. At the 3' end, functions as a processivity factor which stimulates the activity of the viral poly(A) polymerase VP55 that creates mRNA's poly(A) tail. In the presence of VP39, VP55 does not dissociate from the RNA allowing tail elongation to around 250 adenylates.<ref>PMID:1313572</ref> <ref>PMID:1670500</ref> <ref>PMID:12359447</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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==See Also==
==See Also==
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*[[Poly(A) Polymerase|Poly(A) Polymerase]]
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*[[Poly(A) polymerase 3D structures|Poly(A) polymerase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Polynucleotide adenylyltransferase]]
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[[Category: Vaccinia virus WR]]
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[[Category: Vaccw]]
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[[Category: Gershon PD]]
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[[Category: Gershon, P D]]
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[[Category: Hodel AE]]
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[[Category: Hodel, A E]]
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[[Category: Quiocho FA]]
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[[Category: Quiocho, F A]]
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[[Category: Methyltransferase]]
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[[Category: Mrna processing]]
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[[Category: Rna cap]]
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[[Category: Transcription]]
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[[Category: Vaccinia]]
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Current revision

DC26 MUTANT OF VACCINIA VIRUS PROTEIN VP39 IN COMPLEX WITH S-ADENOSYLHOMOCYSTEINE

PDB ID 1vp9

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