Interaction between N-terminal loop and beta-scaffold of photoactive yellow protein.

Abstract:

:During the photoreaction cycle of photoactive yellow protein (PYP), a physiologically active intermediate (PYP(M)) is formed as a consequence of global protein conformational change. Previous studies have demonstrated that the photocycle of PYP is regulated by the N-terminal loop region, which is located across the central beta-sheet from the p-coumaric acid chromophore. In this paper, the hydrophobic interaction between N-terminal loop and beta-sheet was studied by characterizing PYP mutants of the hydrophobic residues. The rate constants and structural changes of the photocycle of L15A and L23A possibly participating in such an interaction were more similar to wild-type than F6A, showing that the CH/pi interaction between Phe6 and Lys123 is the most essential as reported previously. To better understand the interactions between N-terminal tail and beta-sheet of PYP, Phe6 and Phe121 were replaced by Cys and linked by a disulfide bond. Since the photocycle kinetics, structural change and thermal stability of F6C/F121C were similar to F6A, the CH/pi interaction between Phe6 and Lys123 is not substitutable. It is likely that the detachment of position 6 from position 123 substantially alters the nature of PYP.

journal_name

Photochem Photobiol

authors

Harigai M,Kataoka M,Imamoto Y

doi

10.1111/j.1751-1097.2008.00375.x

subject

Has Abstract

pub_date

2008-07-01 00:00:00

pages

1031-7

issue

4

eissn

0031-8655

issn

1751-1097

pii

PHP375

journal_volume

84

pub_type

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