NS5B: Difference between revisions

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<applet load='2HAI_catalytic3.pdb' size='400' frame='true' align='right' caption='Figure 1. PDB ID 2HAI' />NS5B is the RNA dependent RNA polymerase of Hepatitis C virus. NS5B, like other RNA dependent RNA polymerases, is error prone. This viral RNA replicase is of approximately a million times lower fidelity than a replicative prokayrotic or eukaryotic DNA polymerase. This is due in part to the fact that NS5B contains no exonuclease or proofreading domain. IN NS5B two divalent cations coordinated by carboxyl groups (as seen in DNA polymerases) catalyze the polymerization of monomers of RNA triphosphates to extend a primer strand, that may have initiated ''de novo''. In the case of NS5B the residues that coordinate divalent cations (Mg2+ or Mn2+ ''in vitro'') are the three

<applet load='2HAI_catalytic3.pdb' size='400' frame='true' align='right' caption='Figure 1. PDB ID 2HAI' />NS5B is the RNA dependent RNA polymerase of Hepatitis C virus. NS5B, like other RNA dependent RNA polymerases, is error prone. This viral RNA replicase is of approximately a million times lower fidelity than a replicative prokayrotic or eukaryotic DNA polymerase. This is due in part to the fact that NS5B contains no exonuclease or proofreading domain. IN NS5B two divalent cations coordinated by carboxyl groups (as seen in DNA polymerases) catalyze the polymerization of monomers of RNA triphosphates to extend a primer strand, that may have initiated ''de novo''. In the case of NS5B the residues that coordinate divalent cations (Mg2+ or Mn2+ ''in vitro'') are the three <scene name='NS5B/Native_ns5b/4'>active site aspartates (220, 318 and 319)</scene> seen here.

<scene name='NS5B/Native_ns5b/4'>active site aspartates (220, 318 and 319)</scene> seen here.

Though Hepatitis C virus is of the Flaviviridae family the structure of NS5B is similar to the polymerase of bacteriophage Φ 6. The similarity to the bacteriophage polymerase is due to NS5B containing a fully encircled active site. Like many template-dependent nucleotide polymerases, NS5B can be visualized similar to a right hand. NS5B contains several

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-<applet load='2HAI_catalytic3.pdb' size='400' frame='true' align='right' caption='Figure 1. PDB ID 2HAI' />NS5B is the RNA dependent RNA polymerase of Hepatitis C virus. NS5B, like other RNA dependent RNA polymerases, is error prone. This viral RNA replicase is of approximately a million times lower fidelity than a replicative prokayrotic or eukaryotic DNA polymerase. This is due in part to the fact that NS5B contains no exonuclease or proofreading domain. IN NS5B two divalent cations coordinated by carboxyl groups (as seen in DNA polymerases) catalyze the polymerization of monomers of RNA triphosphates to extend a primer strand, that may have initiated ''de novo''. In the case of NS5B the residues that coordinate divalent cations (Mg2+ or Mn2+ ''in vitro'') are the three
+<applet load='2HAI_catalytic3.pdb' size='400' frame='true' align='right' caption='Figure 1. PDB ID 2HAI' />NS5B is the RNA dependent RNA polymerase of Hepatitis C virus. NS5B, like other RNA dependent RNA polymerases, is error prone. This viral RNA replicase is of approximately a million times lower fidelity than a replicative prokayrotic or eukaryotic DNA polymerase. This is due in part to the fact that NS5B contains no exonuclease or proofreading domain. IN NS5B two divalent cations coordinated by carboxyl groups (as seen in DNA polymerases) catalyze the polymerization of monomers of RNA triphosphates to extend a primer strand, that may have initiated ''de novo''. In the case of NS5B the residues that coordinate divalent cations (Mg2+ or Mn2+ ''in vitro'') are the three <scene name='NS5B/Native_ns5b/4'>active site aspartates (220, 318 and 319)</scene> seen here.
-<scene name='NS5B/Native_ns5b/4'>active site aspartates (220, 318 and 319)</scene> seen here.
 Though Hepatitis C virus is of the Flaviviridae family the structure of NS5B is similar to the polymerase of bacteriophage Φ 6. The similarity to the bacteriophage polymerase is due to NS5B containing a fully encircled active site. Like many template-dependent nucleotide polymerases, NS5B can be visualized similar to a right hand. NS5B contains several