Bacterial RNA polymerase.
The recently determined crystal structure of a bacterial core RNA polymerase (RNAP) provides the first glimpse of this family of evolutionarily conserved cellular RNAPs. Using the structure as a framework, a consistent picture of protein-nucleic acid interactions in transcription complexes has been accumulated from cross-linking experiments. The molecule can be viewed as a molecular machine, with distinct structural features hypothesized to perform specific functions. Comparison with the alpha-carbon backbone of a eukaryotic RNAP reveals close structural similarity.
Darst
S A
SA
The Rockefeller University, Box 224, 1230 York Avenue, New York, NY 10021, USA. darst@rockefeller.edu
D019843:Archaeal Proteins / Q000737:chemistry / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D004247:DNA / Q000737:chemistry / Q000378:metabolism; D012321:DNA-Directed RNA Polymerases / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D011487:Protein Conformation; D012313:RNA / Q000737:chemistry / Q000378:metabolism; D014158:Transcription, Genetic
D019843:Archaeal Proteins; D001426:Bacterial Proteins; D012313:RNA; D004247:DNA; D012321:DNA-Directed RNA Polymerases