4ckc

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{{STRUCTURE_4ckc| PDB=4ckc | SCENE= }}
 
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===Vaccinia virus capping enzyme complexed with SAH (monoclinic form)===
 
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{{ABSTRACT_PUBMED_24607143}}
 
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==Function==
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==Vaccinia virus capping enzyme complexed with SAH (monoclinic form)==
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[[http://www.uniprot.org/uniprot/MCEL_VACCW MCEL_VACCW]] Catalytic subunit of the mRNA capping enzyme which catalyzes three enzymatic reactions: the 5' triphosphate end of the pre-mRNA is hydrolyzed to a diphosphate by RNA 5' triphosphatase; the diphosphate RNA end is capped with GMP by RNA guanylyltransferase and the GpppN cap is methylated by RNA (guanine-N7) methyltransferase. Heterodimeric mRNA capping enzyme catalyzes the linkage of a N7-methyl-guanosine moiety to the first transcribed nucleotide (cap 0 structure), whereas the polymerase associated VP39 is responsible for a second methylation at the 2'-O position of the ribose (cap 1 structure).<ref>PMID:18295814</ref> <ref>PMID:18455214</ref> <ref>PMID:18256245</ref> The heterodimeric enzyme is also involved in early viral gene transcription termination and intermediate viral gene transcription initiation. Early gene transcription termination requires the termination factor VTF, the DNA-dependent ATPase NPH-I and the Rap94 subunit of the viral RNA polymerase, as well as the presence of a specific termination motif. Binds, together with RAP94, to the termination motif 5'-UUUUUNU-3' in the nascent early mRNA.<ref>PMID:18295814</ref> <ref>PMID:18455214</ref> <ref>PMID:18256245</ref> [[http://www.uniprot.org/uniprot/MCES_VACCW MCES_VACCW]] Regulatory subunit of the mRNA cap enzyme which stabilizes the catalytic subunit and enhances its methyltransferase activity through an allosteric mechanism. Heterodimeric mRNA capping enzyme catalyzes the linkage of a N7-methyl-guanosine moiety to the first transcribed nucleotide (cap 0 structure), whereas the polymerase associated VP39 is responsible for a second methylation at the 2'-O position of the ribose (cap 1 structure).<ref>PMID:2552660</ref> <ref>PMID:18295814</ref> <ref>PMID:18455214</ref> The heterodimeric enzyme is also involved in early viral gene transcription termination and intermediate viral gene transcription initiation. Early gene transcription termination requires the termination factor VTF, the DNA-dependent ATPase NPH-I and the Rap94 subunit of the viral RNA polymerase, as well as the presence of a specific termination motif. Binds, together with RAP94, to the termination motif 5'-UUUUUNU-3' in the nascent early mRNA.<ref>PMID:2552660</ref> <ref>PMID:18295814</ref> <ref>PMID:18455214</ref>
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<StructureSection load='4ckc' size='340' side='right'caption='[[4ckc]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4ckc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Vaccinia_virus Vaccinia virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CKC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CKC FirstGlance]. <br>
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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]] 2.9&#8491;</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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ckc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ckc OCA], [https://pdbe.org/4ckc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ckc RCSB], [https://www.ebi.ac.uk/pdbsum/4ckc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ckc ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MCEL_VACCW MCEL_VACCW] Catalytic subunit of the mRNA capping enzyme which catalyzes three enzymatic reactions: the 5' triphosphate end of the pre-mRNA is hydrolyzed to a diphosphate by RNA 5' triphosphatase; the diphosphate RNA end is capped with GMP by RNA guanylyltransferase and the GpppN cap is methylated by RNA (guanine-N7) methyltransferase. Heterodimeric mRNA capping enzyme catalyzes the linkage of a N7-methyl-guanosine moiety to the first transcribed nucleotide (cap 0 structure), whereas the polymerase associated VP39 is responsible for a second methylation at the 2'-O position of the ribose (cap 1 structure).<ref>PMID:18295814</ref> <ref>PMID:18455214</ref> <ref>PMID:18256245</ref> The heterodimeric enzyme is also involved in early viral gene transcription termination and intermediate viral gene transcription initiation. Early gene transcription termination requires the termination factor VTF, the DNA-dependent ATPase NPH-I and the Rap94 subunit of the viral RNA polymerase, as well as the presence of a specific termination motif. Binds, together with RAP94, to the termination motif 5'-UUUUUNU-3' in the nascent early mRNA.<ref>PMID:18295814</ref> <ref>PMID:18455214</ref> <ref>PMID:18256245</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Vaccinia virus capping enzyme is a heterodimer of D1 (844 aa) and D12 (287 aa) polypeptides that executes all three steps in m(7)GpppRNA synthesis. The D1 subunit comprises an N-terminal RNA triphosphatase (TPase)-guanylyltransferase (GTase) module and a C-terminal guanine-N7-methyltransferase (MTase) module. The D12 subunit binds and allosterically stimulates the MTase module. Crystal structures of the complete D1D12 heterodimer disclose the TPase and GTase as members of the triphosphate tunnel metalloenzyme and covalent nucleotidyltransferase superfamilies, respectively, albeit with distinctive active site features. An extensive TPase-GTase interface clamps the GTase nucleotidyltransferase and OB-fold domains in a closed conformation around GTP. Mutagenesis confirms the importance of the TPase-GTase interface for GTase activity. The D1D12 structure complements and rationalizes four decades of biochemical studies of this enzyme, which was the first capping enzyme to be purified and characterized, and provides new insights into the origins of the capping systems of other large DNA viruses.
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==About this Structure==
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Crystal structure of vaccinia virus mRNA capping enzyme provides insights into the mechanism and evolution of the capping apparatus.,Kyrieleis OJ, Chang J, de la Pena M, Shuman S, Cusack S Structure. 2014 Mar 4;22(3):452-65. doi: 10.1016/j.str.2013.12.014. PMID:24607143<ref>PMID:24607143</ref>
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[[4ckc]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CKC OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<ref group="xtra">PMID:024607143</ref><references group="xtra"/><references/>
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</div>
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[[Category: Chang, J.]]
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<div class="pdbe-citations 4ckc" style="background-color:#fffaf0;"></div>
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[[Category: Cusack, S.]]
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== References ==
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[[Category: Kyrieleis, O J.P.]]
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<references/>
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[[Category: Pena, M de la.]]
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__TOC__
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[[Category: Shuman, S.]]
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</StructureSection>
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[[Category: Transferase-hydrolase complex]]
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[[Category: Large Structures]]
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[[Category: Trifunctional vaccinia virus mrna capping enzyme]]
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[[Category: Vaccinia virus]]
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[[Category: Chang J]]
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[[Category: Cusack S]]
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[[Category: Kyrieleis OJP]]
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[[Category: Shuman S]]
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[[Category: De la Pena M]]

Current revision

Vaccinia virus capping enzyme complexed with SAH (monoclinic form)

PDB ID 4ckc

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