2pgg: Difference between revisions

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[[Image:2pgg.gif|left|200px]]
{{Seed}}
[[Image:2pgg.png|left|200px]]


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{{STRUCTURE_2pgg|  PDB=2pgg  |  SCENE=  }}  
{{STRUCTURE_2pgg|  PDB=2pgg  |  SCENE=  }}  


'''Crystal Structure of a Birnavirus (IBDV) RNA-dependent RNA Polymerase VP1'''
===Crystal Structure of a Birnavirus (IBDV) RNA-dependent RNA Polymerase VP1===




==Overview==
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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 line below this paragraph, {{ABSTRACT_PUBMED_17456597}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 17456597 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17456597}}


==About this Structure==
==About this Structure==
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[[Category: Polymerase]]
[[Category: Polymerase]]
[[Category: Rdrp]]
[[Category: Rdrp]]
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