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| {{STRUCTURE_1ra6| PDB=1ra6 | SCENE= }} | | {{STRUCTURE_1ra6| PDB=1ra6 | SCENE= }} |
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| '''Poliovirus Polymerase Full Length Apo Structure'''
| | ===Poliovirus Polymerase Full Length Apo Structure=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_15306852}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15306852 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15306852}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Polymerase]] | | [[Category: Polymerase]] |
| [[Category: Rna-dependent]] | | [[Category: Rna-dependent]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:15:53 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:23:12 2008'' |
