3er8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (00:23, 28 December 2023) (edit) (undo)
 
(4 intermediate revisions not shown.)
Line 1: Line 1:
-
{{STRUCTURE_3er8| PDB=3er8 | SCENE= }}
 
-
===Crystal structure of the heterodimeric vaccinia virus mRNA polyadenylate polymerase complex with two fragments of RNA===
 
-
{{ABSTRACT_PUBMED_19446524}}
 
-
==Function==
+
==Crystal structure of the heterodimeric vaccinia virus mRNA polyadenylate polymerase complex with two fragments of RNA==
-
[[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.
+
<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 [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=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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.18&#8491;</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 ==
 +
[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 ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/er/3er8_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3er8 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== 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.
-
==About this Structure==
+
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<ref>PMID:19446524</ref>
-
[[3er8]] is a 8 chain structure with sequence from [http://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=3ER8 OCA].
+
-
==See Also==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
*[[Poly(A) Polymerase|Poly(A) Polymerase]]
+
</div>
 +
<div class="pdbe-citations 3er8" style="background-color:#fffaf0;"></div>
-
==Reference==
+
==See Also==
-
<ref group="xtra">PMID:019446524</ref><references group="xtra"/><references/>
+
*[[Poly(A) polymerase 3D structures|Poly(A) polymerase 3D structures]]
-
[[Category: Vaccinia virus wr]]
+
== References ==
-
[[Category: Gershon, P D.]]
+
<references/>
-
[[Category: Li, C.]]
+
__TOC__
-
[[Category: Li, H]]
+
</StructureSection>
-
[[Category: Poulos, T L.]]
+
[[Category: Large Structures]]
-
[[Category: Zhou, S.]]
+
[[Category: Vaccinia virus WR]]
-
[[Category: Heterodimer]]
+
[[Category: Gershon PD]]
-
[[Category: Methyltransferase]]
+
[[Category: Li C]]
-
[[Category: Mrna capping]]
+
[[Category: Li H]]
-
[[Category: Mrna processing]]
+
[[Category: Poulos TL]]
-
[[Category: Nucleotidyltransferase]]
+
[[Category: Zhou S]]
-
[[Category: Polyadenylate polymerase]]
+
-
[[Category: Poxvirus]]
+
-
[[Category: Processivity]]
+
-
[[Category: Rna complex]]
+
-
[[Category: Rna protein complex]]
+
-
[[Category: S-adenosyl-l-methionine]]
+
-
[[Category: Transcription]]
+
-
[[Category: Transferase]]
+
-
[[Category: Transferase-dna]]
+
-
[[Category: Transferase/dna]]
+
-
[[Category: Translocation]]
+

Current revision

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

PDB ID 3er8

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools