1raj | pdb_00001raj

Poliovirus Polymerase with a 68 residue N-terminal truncation

spinqualitylabelsall models 1raj, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1raj is a 1 chain structure with sequence from Human poliovirus 1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1rdr, 1ra6, 1ra7, 1tql Gene: 3D (Human poliovirus 1) Activity: RNA-directed RNA polymerase, with EC number 2.7.7.48 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The active RNA-dependent RNA polymerase of poliovirus, 3Dpol, is generated by cleavage of the 3CDpro precursor protein, a protease that has no polymerase activity despite containing the entire polymerase domain. By intentionally disrupting a known and persistent crystal packing interaction, we have crystallized the poliovirus polymerase in a new space group and solved the complete structure of the protein at 2.0 A resolution. It shows that the N-terminus of fully processed 3Dpol is buried in a surface pocket where it makes hydrogen bonds that act to position Asp238 in the active site. Asp238 is an essential residue that selects for the 2' OH group of substrate rNTPs, as shown by a 2.35 A structure of a 3Dpol-GTP complex. Mutational, biochemical, and structural data further demonstrate that 3Dpol activity is exquisitely sensitive to mutations at the N-terminus. This sensitivity is the result of allosteric effects where the structure around the buried N-terminus directly affects the positioning of Asp238 in the active site. Structural basis for proteolysis-dependent activation of the poliovirus RNA-dependent RNA polymerase.,Thompson AA, Peersen OB EMBO J. 2004 Sep 1;23(17):3462-71. Epub 2004 Aug 12. PMID:15306852 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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