Light-induced Trpin/Metout Switching During BLUF Domain Activation in ATP-bound Photoactivatable Adenylate Cyclase OaPAC

Anaïs Chretien, Marius F. Nagel,Sabine Botha,Raphaël de Wijn,Lea Brings,Katerina Dörner,Huijong Han,Jayanath C.P. Koliyadu,Romain Letrun,Adam Round, Tokushi Sato,Christina Schmidt, Radu-Costin Secareanu,David von Stetten,Mohammad Vakili, Agnieszka Wrona,Richard Bean,Adrian Mancuso,Joachim Schulz,Arwen R. Pearson

bioRxiv (Cold Spring Harbor Laboratory)（2024）

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摘要

•Investigation of the light excitation and signal transduction of photoreceptor OaPAC.•Structural details of ATP binding in active site of adenylate cyclase domain.•Time-resolved crystallography highlights the initial events around the chromophore.•Late reaction state reveals Trpin/Metout switching during BLUF domain activation.•Better understanding of BLUF activation and signal transmission to effector domain.

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关键词

time-resolved crystallography,photoreceptor,BLUF domain,light excitation,signal transduction

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