Structural and dynamic changes of photoactive yellow protein during its photocycle in solution.
Light irradiation of photoactive yellow protein (PYP) induces a photocycle, in which red-shifted (pR) and blue-shifted (pB) intermediates have been characterized. An NMR study of the long-lived pB intermediate now reveals that it exhibits a large degree of disorder and exists as a family of multiple conformers that exchange on a millisecond time scale. This shows that the behavior of PYP in solution is different from what has been observed in the crystalline state. Furthermore, differential refolding to ground state pG is observed, whereby the central beta-sheet and parts of the helical structure are formed first and the region around the chromophore at a later stage.
Rubinstenn
G
G
Bijovet Center for Biomolecular Research, Utrecht University, The Netherlands.
Vuister
G W
GW
Mulder
F A
FA
Düx
P E
PE
Boelens
R
R
Hellingwerf
K J
KJ
Kaptein
R
R
D001426:Bacterial Proteins / Q000737:chemistry* / Q000528:radiation effects; D002841:Chromatiaceae / Q000737:chemistry; D007834:Lasers; D019906:Nuclear Magnetic Resonance, Biomolecular; D020283:Photoreceptors, Microbial; D011487:Protein Conformation
D001426:Bacterial Proteins; D020283:Photoreceptors, Microbial; C050162:photoactive yellow protein, Bacteria