時分割タンパク質結晶学によるDNAポリメラーゼηのヌクレオチド転移反応の可視化
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We visualized the course of nucleotidyl transfer reaction by human DNA polymerase η (Pol η) using time resolved protein crystallography. The reaction was initiated by exposing Pol η-DNA-dATP crystals to 1 mM Mg2+ at pH 7.0 and stopped at various time points by freezing. The substrates and two Mg2+ ions are aligned for reaction within 40 s. Transient electron densities indicate that deprotonation and an accompanying C2-endo to C3-endo conversion of the nucleophile 3-OH are rate limiting. A third Mg2+ ion, which arrives with the new bond and stabilizes the intermediate state, may be an unappreciated feature of the two-metal-ion mechanism.
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- 時分割タンパク質結晶学によるDNAポリメラーゼηのヌクレオチド転移反応の可視化