2pgg

<StructureSection load='2pgg' size='340' side='right' caption='[[2pgg]], [[Resolution|resolution]] 2.50&Aring;' scene=''>

<table><tr><td colspan='2'>[[2pgg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Avian_infectious_bursal_disease_virus Avian infectious bursal disease virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PGG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PGG FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10995 Avian infectious bursal disease virus])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RNA-directed_RNA_polymerase RNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.48 2.7.7.48] </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=2pgg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pgg OCA], [http://pdbe.org/2pgg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2pgg RCSB], [http://www.ebi.ac.uk/pdbsum/2pgg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2pgg ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/RDRP_IBDV RDRP_IBDV]] RNA-dependent RNA polymerase which is found both free and covalently attached to the genomic RNA. May also contain guanylyl and methyl transferase activities (By similarity).

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== Publication Abstract from PubMed ==

Single-subunit polymerases are universally encoded in both cellular organisms and viruses. Their three-dimensional structures have the shape of a right-hand with the active site located in the palm region, which has a topology similar to that of the RNA recognition motif (RRM) found in many RNA-binding proteins. Considering that polymerases have well conserved structures, it was surprising that the RNA-dependent RNA polymerases from birnaviruses, a group of dsRNA viruses, have their catalytic motifs arranged in a permuted order in sequence. Here we report the 2.5 A structure of a birnavirus VP1 in which the polymerase palm subdomain adopts a new active site topology that has not been previously observed in other polymerases. In addition, the polymerase motif C of VP1 has the sequence of -ADN-, a highly unusual feature for RNA-dependent polymerases. Through site-directed mutagenesis, we have shown that changing the VP1 motif C from -ADN- to -GDD- results in a mutant with an increased RNA synthesis activity. Our results indicate that the active site topology of VP1 may represent a newly developed branch in polymerase evolution, and that birnaviruses may have acquired the -ADN- mutation to control their growth rate.

The structure of a birnavirus polymerase reveals a distinct active site topology.,Pan J, Vakharia VN, Tao YJ Proc Natl Acad Sci U S A. 2007 May 1;104(18):7385-90. Epub 2007 Apr 24. PMID:17456597<ref>PMID:17456597</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 2pgg" style="background-color:#fffaf0;"></div>

*[[RNA polymerase|RNA polymerase]]

[[Category: Avian infectious bursal disease virus]]

[[Category: RNA-directed RNA polymerase]]

[[Category: Pan, J]]

[[Category: Tao, Y J]]

[[Category: Vakharia, V N]]

[[Category: Transferase]]