The role of the N‐terminal domain of photoactive yellow protein in the transient partial unfolding during signalling state formation

FEBS Letters

van Stokkum, Ivo H¹  van der Horst, Michael A²  Crielaard, Wim²  Hellingwerf, Klaas J² 

[1] Department of Physics Applied Computer Science, Division of Physics and Astronomy, Faculty of Sciences, Vrije Universiteit, de Boelelaan 1081, 1081 HV Amsterdam, The Netherlands;Laboratory for Microbiology, Swammerdam Institute for Life Sciences, BioCentrum, University of Amsterdam, Nieuwe Achtergracht 166, 1018 WV Amsterdam, The Netherlands

关键词: Photocycle kinetics;    Arrhenius plot;    Cooperativity;    Titration curve;    Truncated protein;    Specific heat capacity;    Cooperativity;    PYP;    photoactive yellow protein;    pG;    ground state of the photocycle of PYP;    absorbing at 446 nm;    pB;    blue-shifted photocycle intermediate;    which is the presumed signalling state;   

DOI  :  10.1016/S0014-5793(01)02427-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

It is shown that the N-terminal domain of photoactive yellow protein (PYP), which appears relatively independently folded in the ground state of the protein, plays a key role in the transient unfolding during signalling state formation: genetic truncation of the N-terminal domain of PYP significantly decreases the extent of cooperativity of the titration curve that describes chromophore protonation in the ground state of PYP, which is in agreement with the notion that the N-terminal domain is linked through a hydrogen-bonding network with the chromophore-containing domain of the protein. Furthermore, deletion of the N-terminal domain completely abolishes the non-linearity of the Arrhenius plot of the rate of ground state recovery.

【 授权许可】

Unknown