3er8

From Proteopedia

(Difference between revisions)

Revision as of 19:45, 20 October 2021

Crystal structure of the heterodimeric vaccinia virus mRNA polyadenylate polymerase complex with two fragments of RNA

Structural highlights

3er8 is a 8 chain structure with sequence from Vaccw. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2ga9, 3er9, 3erc
Gene:	PAPS, VACWR095, F9 (VACCW), PAPL, VACWR057, E1L (VACCW)
Activity:	mRNA (nucleoside-2'-O)-methyltransferase, with EC number 2.1.1.57
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2] ^[3] [PAP1_VACCW] Polymerase that creates the 3'-poly(A) tail of mRNA's.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Vaccinia virus protein VP55 translocates continuously with respect to single-stranded nucleic acid while extending its 3'end. Here, all key sites of polymerase-primer interaction were identified, demonstrating the wrapping or looping of polyadenylation primer around the polymerase during translocation. Side-chain substitutions at one of the sites indicated its requirement for tail extension beyond approximately 12 nucleotides in length, and conformational changes observed upon oligonucleotide binding suggested allosteric connectivity during translocation. Conformational changes in VP39 upon VP55 binding suggested that, within the VP55-VP39 complex, VP39's mRNA 5' cap binding site closes. The crystallographic structure showed a PAPase catalytic center without side-chain substitutions, possessing two metal ions and with all known reactive and catalytic groups represented, fitting a classical two-metal ion mechanism for phosphoryl transfer.

Polymerase translocation with respect to single-stranded nucleic acid: looping or wrapping of primer around a poly(A) polymerase.,Li C, Li H, Zhou S, Sun E, Yoshizawa J, Poulos TL, Gershon PD Structure. 2009 May 13;17(5):680-9. PMID:19446524^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Schnierle BS, Gershon PD, Moss B. Cap-specific mRNA (nucleoside-O2'-)-methyltransferase and poly(A) polymerase stimulatory activities of vaccinia virus are mediated by a single protein. Proc Natl Acad Sci U S A. 1992 Apr 1;89(7):2897-901. PMID:1313572
↑ Gershon PD, Ahn BY, Garfield M, Moss B. Poly(A) polymerase and a dissociable polyadenylation stimulatory factor encoded by vaccinia virus. Cell. 1991 Sep 20;66(6):1269-78. PMID:1670500
↑ Latner DR, Thompson JM, Gershon PD, Storrs C, Condit RC. The positive transcription elongation factor activity of the vaccinia virus J3 protein is independent from its (nucleoside-2'-O-) methyltransferase and poly(A) polymerase stimulatory functions. Virology. 2002 Sep 15;301(1):64-80. PMID:12359447
↑ Li C, Li H, Zhou S, Sun E, Yoshizawa J, Poulos TL, Gershon PD. Polymerase translocation with respect to single-stranded nucleic acid: looping or wrapping of primer around a poly(A) polymerase. Structure. 2009 May 13;17(5):680-9. PMID:19446524 doi:10.1016/j.str.2009.03.012

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3er8"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the heterodimeric vaccinia virus mRNA polyadenylate polymerase complex with two fragments of RNA==
-<StructureSection load='3er8' size='340' side='right' caption='[[3er8]], [[Resolution|resolution]] 3.18&Aring;' scene=''>
+<StructureSection load='3er8' size='340' side='right'caption='[[3er8]], [[Resolution|resolution]] 3.18&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3er8]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Vaccw Vaccw]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ER8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ER8 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3er8]] is a 8 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=3ER8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ER8 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ga9|2ga9]], [[3er9|3er9]], [[3erc|3erc]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2ga9|2ga9]], [[3er9|3er9]], [[3erc|3erc]]</div></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PAPS, VACWR095, F9 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10254 VACCW]), PAPL, VACWR057, E1L ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10254 VACCW])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PAPS, VACWR095, F9 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10254 VACCW]), PAPL, VACWR057, E1L ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10254 VACCW])</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/mRNA_(nucleoside-2'-O)-methyltransferase mRNA (nucleoside-2'-O)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.57 2.1.1.57] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/mRNA_(nucleoside-2'-O)-methyltransferase mRNA (nucleoside-2'-O)-methyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.57 2.1.1.57] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3er8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3er8 OCA], [http://pdbe.org/3er8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3er8 RCSB], [http://www.ebi.ac.uk/pdbsum/3er8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3er8 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=3er8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3er8 OCA], [https://pdbe.org/3er8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3er8 RCSB], [https://www.ebi.ac.uk/pdbsum/3er8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3er8 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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>  [[http://www.uniprot.org/uniprot/PAP1_VACCW PAP1_VACCW]] Polymerase that creates the 3'-poly(A) tail of mRNA's.
+[[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>  [[https://www.uniprot.org/uniprot/PAP1_VACCW PAP1_VACCW]] Polymerase that creates the 3'-poly(A) tail of mRNA's.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 30: / Line 30: @@
 </div>
 <div class="pdbe-citations 3er8" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Poly(A) Polymerase|Poly(A) Polymerase]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Vaccw]]
 [[Category: Gershon, P D]]

3er8

From Proteopedia

Revision as of 19:45, 20 October 2021

Crystal structure of the heterodimeric vaccinia virus mRNA polyadenylate polymerase complex with two fragments of RNA

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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