
New structures of RNA polymerase II (pol II) transcribing complexes reveal a likely key to transcription. The trigger loop swings beneath a correct nucleoside triphosphate (NTP) in the nucleotide addition site, closing off the active center and forming an extensive network of interactions with the NTP base, sugar, phosphates, and additional pol II residues. A histidine side chain in the trigger loop, precisely positioned by these interactions, may literally "trigger" phosphodiester bond formation. Recognition and catalysis are thus coupled, ensuring the fidelity of transcription.
Models, Molecular, Amanitins, Binding Sites, Transcription, Genetic, Biochemistry, Genetics and Molecular Biology(all), Nucleotides, Protein Conformation, Molecular Sequence Data, DNA, Saccharomyces cerevisiae, Crystallography, X-Ray, Catalysis, Substrate Specificity, Nucleic Acid Conformation, Histidine, Magnesium, Amino Acid Sequence, RNA Polymerase II
Models, Molecular, Amanitins, Binding Sites, Transcription, Genetic, Biochemistry, Genetics and Molecular Biology(all), Nucleotides, Protein Conformation, Molecular Sequence Data, DNA, Saccharomyces cerevisiae, Crystallography, X-Ray, Catalysis, Substrate Specificity, Nucleic Acid Conformation, Histidine, Magnesium, Amino Acid Sequence, RNA Polymerase II
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