RNA polymerase

From Proteopedia

Template:STRUCTURE 3m3y

RNA polymerase (RNAP, DNA primase, dnaG) catalyzes the addition of nucleotides to RNA during transcription. DNA primase (DNAP) is RNAP which catalyzes the synthesis of the RNA primer which complements an ssDNA template and initiates DNA synthesis. dnaG is a bacterial primase. Polymerase acidic protein (PAP) is an Influenza virus RNA polymerase. It is implicated in endonuclease cleavage of RNA primers. (1qln; blue: nontemplate strand; cyan: template strand; red:RNA). See also Transcription and RNA Processing.
For RNA polymerase from bacteriophage T7 see

• Molecular Playground/T7 RNAP Conformations
  
• User:Luis E Ramirez-Tapia/T7 RNA polymerase
  
• Molecular Playground/T7 RNA Polymerase (7 mer int).
  

For RNA-dependent RNA polymerase from Hepatitis C virus - NS5B - see

• NS5B.
  

For DNA-dependent RNA polymerase see

• Molecular Playground/Human mtRNA pol.
  

For the Thermus thermophilus β' subunit see

• Beta-Prime Subunit of Bacterial RNA Polymerase
  

For the influenza virus RNA-dependent RNA polymerase PB2 and PA homology model and sequence alignment see

• User:Michael Strong/H1N1/PB2
  
• User:Michael Strong/H1N1/PB2/MSA
  
• User:Michael Strong/H1N1/PA
  
• User:Michael Strong/H1N1/PA/MSA

3D Structures of RNA polymerase

Updated on 09-December-2014

• Created with the participation of Craig T Martin.