A structural pathway for signaling in the E46Q mutant of photoactive yellow protein

Sudarshan Rajagopal, Spencer Anderson, Vukica Srajer, Marius Schmidt, Reinhard Pahl, Keith Moffat

Research output: Contribution to journalArticlepeer-review

64 Scopus citations


In the bacterial photoreceptor photoactive yellow protein (PYP), absorption of blue light by its chromophore leads to a conformational change in the protein associated with differential signaling activity, as it executes a reversible photocycle. Time-resolved Laue crystallography allows structural snapshots (as short as 150 ps) of high crystallographic resolution (∼1.6 Å) to be taken of a protein as it functions. Here, we analyze by singular value decomposition a comprehensive time-resolved crystallographic data set of the E46Q mutant of PYP throughout the photocycle spanning 10 ns-100 ms. We identify and refine the structures of five distinct intermediates and provide a plausible chemical kinetic mechanism for their inter conversion. A clear structural progression is visible in these intermediates, in which a signal generated at the chromophore propagates through a distinct structural pathway of conserved residues and results in structural changes near the N terminus, over 20 Å distant from the chromophore.

Original languageEnglish (US)
Pages (from-to)55-63
Number of pages9
Issue number1
StatePublished - Jan 2005

ASJC Scopus subject areas

  • Molecular Biology
  • Structural Biology


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