2gaf

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[[Image:2gaf.gif|left|200px]]<br /><applet load="2gaf" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2gaf, resolution 2.400&Aring;" />
 
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'''Crystal Structure of the Vaccinia Polyadenylate Polymerase Heterodimer (apo form)'''<br />
 
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==Overview==
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==Crystal Structure of the Vaccinia Polyadenylate Polymerase Heterodimer (apo form)==
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<StructureSection load='2gaf' size='340' side='right'caption='[[2gaf]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2gaf]] is a 2 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=2GAF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GAF 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]] 2.4&#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=MSE:SELENOMETHIONINE'>MSE</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=2gaf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gaf OCA], [https://pdbe.org/2gaf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gaf RCSB], [https://www.ebi.ac.uk/pdbsum/2gaf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gaf ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q1PIV4_9POXV Q1PIV4_9POXV] 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 OPG063 that creates mRNA's poly(A) tail. In the presence of OPG102, OPG063 does not dissociate from the RNA allowing tail elongation to around 250 adenylates.[ARBA:ARBA00034661][PIRNR:PIRNR003726]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ga/2gaf_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2gaf ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
Polyadenylation of mRNAs in poxviruses, crucial for virion maturation, is carried out by a poly(A) polymerase heterodimer composed of a catalytic component, VP55, and a processivity factor, VP39. The ATP-gamma-S bound and unbound crystal structures of the vaccinia polymerase reveal an unusual architecture for VP55 that comprises of N-terminal, central or catalytic, and C-terminal domains with different topologies and that differs from many polymerases, including the eukaryotic poly(A) polymerases. Residues in the active site of VP55, located between the catalytic and C-terminal domains, make specific interactions with the adenine of the ATP analog, establishing the molecular basis of ATP recognition. VP55's concave surface docks the globular VP39. A model for RNA primer binding that involves all three VP55 domains and VP39 is proposed. The model supports biochemical evidence that VP39 functions as a processivity factor by partially enclosing the RNA primer at the heterodimer interface.
Polyadenylation of mRNAs in poxviruses, crucial for virion maturation, is carried out by a poly(A) polymerase heterodimer composed of a catalytic component, VP55, and a processivity factor, VP39. The ATP-gamma-S bound and unbound crystal structures of the vaccinia polymerase reveal an unusual architecture for VP55 that comprises of N-terminal, central or catalytic, and C-terminal domains with different topologies and that differs from many polymerases, including the eukaryotic poly(A) polymerases. Residues in the active site of VP55, located between the catalytic and C-terminal domains, make specific interactions with the adenine of the ATP analog, establishing the molecular basis of ATP recognition. VP55's concave surface docks the globular VP39. A model for RNA primer binding that involves all three VP55 domains and VP39 is proposed. The model supports biochemical evidence that VP39 functions as a processivity factor by partially enclosing the RNA primer at the heterodimer interface.
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==About this Structure==
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Crystal structures of the vaccinia virus polyadenylate polymerase heterodimer: insights into ATP selectivity and processivity.,Moure CM, Bowman BR, Gershon PD, Quiocho FA Mol Cell. 2006 May 5;22(3):339-49. PMID:16678106<ref>PMID:16678106</ref>
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2GAF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Vaccinia_virus Vaccinia virus]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GAF 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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Crystal structures of the vaccinia virus polyadenylate polymerase heterodimer: insights into ATP selectivity and processivity., Moure CM, Bowman BR, Gershon PD, Quiocho FA, Mol Cell. 2006 May 5;22(3):339-49. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16678106 16678106]
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</div>
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[[Category: Protein complex]]
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<div class="pdbe-citations 2gaf" style="background-color:#fffaf0;"></div>
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[[Category: Vaccinia virus]]
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[[Category: mRNA (nucleoside-2'-O-)-methyltransferase]]
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[[Category: Bowman, B R.]]
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[[Category: Gershon, P D.]]
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[[Category: Moure, C M.]]
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[[Category: Quiocho, F A.]]
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[[Category: heterodimer]]
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[[Category: nucleotidyltransferase]]
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[[Category: polyadenylate polymerase]]
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[[Category: pox virus]]
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[[Category: processivity]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:29:45 2008''
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==See Also==
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*[[Poly(A) polymerase 3D structures|Poly(A) polymerase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Vaccinia virus]]
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[[Category: Bowman BR]]
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[[Category: Gershon PD]]
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[[Category: Moure CM]]
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[[Category: Quiocho FA]]

Current revision

Crystal Structure of the Vaccinia Polyadenylate Polymerase Heterodimer (apo form)

PDB ID 2gaf

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