3mag: Difference between revisions

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{{Seed}}
[[Image:3mag.png|left|200px]]


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==VACCINIA METHYLTRANSFERASE VP39 COMPLEXED WITH M3ADE AND S-ADENOSYLHOMOCYSTEINE==
The line below this paragraph, containing "STRUCTURE_3mag", creates the "Structure Box" on the page.
<StructureSection load='3mag' size='340' side='right'caption='[[3mag]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3mag]] is a 1 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=3MAG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MAG FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#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=3MA:6-AMINO-3-METHYLPURINE'>3MA</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
{{STRUCTURE_3mag| PDB=3mag |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3mag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mag OCA], [https://pdbe.org/3mag PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mag RCSB], [https://www.ebi.ac.uk/pdbsum/3mag PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mag 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/ma/3mag_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=3mag ConSurf].
<div style="clear:both"></div>


===VACCINIA METHYLTRANSFERASE VP39 COMPLEXED WITH M3ADE AND S-ADENOSYLHOMOCYSTEINE===
==See Also==
 
*[[Poly(A) polymerase 3D structures|Poly(A) polymerase 3D structures]]
 
== References ==
<!--
<references/>
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(as it appears on PubMed at http://www.pubmed.gov), where 10377383 is the PubMed ID number.
</StructureSection>
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[[Category: Large Structures]]
{{ABSTRACT_PUBMED_10377383}}
 
==About this Structure==
3MAG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Vaccinia_virus Vaccinia virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MAG OCA].
 
==Reference==
mRNA cap recognition: dominant role of enhanced stacking interactions between methylated bases and protein aromatic side chains., Hu G, Gershon PD, Hodel AE, Quiocho FA, Proc Natl Acad Sci U S A. 1999 Jun 22;96(13):7149-54. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10377383 10377383]
[[Category: Polynucleotide adenylyltransferase]]
[[Category: Single protein]]
[[Category: Vaccinia virus]]
[[Category: Vaccinia virus]]
[[Category: Gershon, P D.]]
[[Category: Gershon PD]]
[[Category: Hodel, A E.]]
[[Category: Hodel AE]]
[[Category: Hu, G.]]
[[Category: Hu G]]
[[Category: Quiocho, F A.]]
[[Category: Quiocho FA]]
[[Category: Methylated adenine]]
[[Category: Methyltransferase]]
[[Category: Mrna processing]]
[[Category: Rna cap analog]]
[[Category: Transcription]]
[[Category: Vaccinia]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul  3 12:54:52 2008''

Latest revision as of 13:24, 21 February 2024

VACCINIA METHYLTRANSFERASE VP39 COMPLEXED WITH M3ADE AND S-ADENOSYLHOMOCYSTEINEVACCINIA METHYLTRANSFERASE VP39 COMPLEXED WITH M3ADE AND S-ADENOSYLHOMOCYSTEINE

Structural highlights

3mag is a 1 chain structure with sequence from Vaccinia virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:,
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]

Evolutionary Conservation

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

See Also

References

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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

3mag, resolution 1.80Å

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