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RNA polymerase
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In molecular biology, RNA polymerase, or more specifically DNA-directed/dependent RNA polymerase, is an enzyme that catalyzes the chemical reactions that synthesize RNA from a DNA template strand.
RNA polymerase hetero 27-mer, human
RNA polymerase hetero 27-mer, human
An electron-micrograph of DNA strands decorated by hundreds of RNAP molecules too small to be resolved. Each RNAP is transcribing an RNA strand, which
An electron-micrograph of DNA strands decorated by hundreds of RNAP molecules too small to be resolved. Each RNAP is transcribing an RNA strand, which can be seen branching off from the DNA. "Begin" indicates the 3′ end of the DNA, where RNAP initiates transcription; "End" indicates the 5′ end, where the longer RNA molecules are completely transcribed.
RNAP from T. aquaticus pictured during elongation. Portions of the enzyme were made transparent so as to make the path of RNA and DNA more clear. The
RNAP from T. aquaticus pictured during elongation. Portions of the enzyme were made transparent so as to make the path of RNA and DNA more clear. The magnesium ion (yellow) is located at the enzyme active site.
T7 RNA polymerase producing a mRNA (green) from a DNA template. The protein is shown as a purple ribbon (PDB: 1MSW​)
T7 RNA polymerase producing a mRNA (green) from a DNA template. The protein is shown as a purple ribbon (PDB: 1MSW​)
DNA polymerase
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A DNA polymerase is a member of a family of enzymes that catalyze the synthesis of DNA molecules from nucleoside triphosphates, the molecular precursors of DNA. These enzymes are essential for DNA rep
RNA polymerase
…a similar core structure and mechanism. The latter is found in phages as well as eukaryotic chloroplasts and mitochondria, and is related to modern DNA polymerases. Eukaryotic and archaeal RNAPs have more subunits than bacterial ones do, and are controlled differently. Bacteria and archaea only have one RNA…
c:o6-methyl-guanine pair in the polymerase-2 basepair position
c:o6-methyl-guanine pair in the polymerase-2 basepair position
crystal structure of rb69 gp43 in complex with dna containing thymine glycol
crystal structure of rb69 gp43 in complex with dna containing thymine glycol
phi29 dna polymerase, orthorhombic crystal form, ssdna complex
phi29 dna polymerase, orthorhombic crystal form, ssdna complex
Structures of archaeal polD and eukaryotic Polα. Not only is the general topology conserved, the two also share a bifunctional primase-and-PCNA-bindin
Structures of archaeal polD and eukaryotic Polα. Not only is the general topology conserved, the two also share a bifunctional primase-and-PCNA-binding PIP-box sequence on the C-terminus, similar to both eukaryotic Polα and Polε.