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6a4v

From Proteopedia

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Current revision (10:30, 27 March 2024) (edit) (undo)
 
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<StructureSection load='6a4v' size='340' side='right'caption='[[6a4v]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='6a4v' size='340' side='right'caption='[[6a4v]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6a4v]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mhv68 Mhv68]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5yx5 5yx5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A4V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A4V FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6a4v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Murid_gammaherpesvirus_4 Murid gammaherpesvirus 4]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5yx5 5yx5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A4V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6A4V FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BNLF1, 49, GAMMAHV.ORF49 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=33708 MHV68])</td></tr>
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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]] 2.2&#8491;</td></tr>
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<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=6a4v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a4v OCA], [http://pdbe.org/6a4v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a4v RCSB], [http://www.ebi.ac.uk/pdbsum/6a4v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a4v ProSAT]</span></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=6a4v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a4v OCA], [https://pdbe.org/6a4v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6a4v RCSB], [https://www.ebi.ac.uk/pdbsum/6a4v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6a4v ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/P88987_MHV68 P88987_MHV68]
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Poly(ADP-ribose) polymerase 1 (PARP-1), an enzyme that modifies nuclear proteins by poly(ADP-ribosyl)ation, regulates various cellular activities and restricts the lytic replication of oncogenic gammaherpesviruses by inhibiting the function of replication and transcription activator (RTA), a key switch molecule of the viral life cycle. A viral PARP-1-interacting protein (vPIP) encoded by murine gammaherpesvirus 68 (MHV-68) orf49 facilitates lytic replication by disrupting interactions between PARP-1 and RTA. Here, the structure of MHV-68 vPIP was determined at 2.2 A resolution. The structure consists of 12 alpha-helices with characteristic N-terminal beta-strands (Nbeta) and forms a V-shaped-twist dimer in the asymmetric unit. Structure-based mutagenesis revealed that Nbeta and the alpha1 helix (residues 2-26) are essential for the nuclear localization and function of vPIP; three residues were then identified (Phe5, Ser12 and Thr16) that were critical for the function of vPIP and its interaction with PARP-1. A recombinant MHV-68 harboring mutations of these three residues showed severely attenuated viral replication both in vitro and in vivo. Moreover, ORF49 of Kaposi's sarcoma-associated herpesvirus also directly interacted with PARP-1, indicating a conserved mechanism of action of vPIPs. The results elucidate the novel molecular mechanisms by which oncogenic gammaherpesviruses overcome repression by PARP-1 using vPIPs.
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Structure-based mechanism of action of a viral poly(ADP-ribose) polymerase 1-interacting protein facilitating virus replication.,Chung WC, Kim J, Kim BC, Kang HR, Son J, Ki H, Hwang KY, Song MJ IUCrJ. 2018 Oct 31;5(Pt 6):866-879. doi: 10.1107/S2052252518013854. eCollection, 2018 Nov 1. PMID:30443370<ref>PMID:30443370</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6a4v" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Mhv68]]
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[[Category: Murid gammaherpesvirus 4]]
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[[Category: Cheong, W C]]
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[[Category: Cheong WC]]
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[[Category: Hwang, K Y]]
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[[Category: Hwang KY]]
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[[Category: Kim, J S]]
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[[Category: Kim JS]]
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[[Category: Song, M J]]
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[[Category: Song MJ]]
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[[Category: Gamma herpesvirus 68 open reading frame 49]]
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[[Category: Replication]]
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Current revision

Open Reading frame 49

PDB ID 6a4v

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