The role of the N-terminal domain of photoactive yellow protein in the transient partial unfolding during signalling state formation.
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.
van der Horst
M A
MA
Laboratory for Microbiology, Swammerdam Institute for Life Sciences, Biocentrum, University of Amsterdam, Nieuwe Achtergracht 166,1018 WV Amsterdam, The Netherlands.
van Stokkum
I H
IH
Crielaard
W
W
Hellingwerf
K J
KJ
D001426:Bacterial Proteins / Q000737:chemistry* / Q000502:physiology*; D020607:Halorhodospira halophila; D006860:Hydrogen Bonding; D006863:Hydrogen-Ion Concentration; D016297:Mutagenesis, Site-Directed; D020283:Photoreceptors, Microbial; D017510:Protein Folding; D017434:Protein Structure, Tertiary / Q000502:physiology; D015398:Signal Transduction / Q000502:physiology*; D013053:Spectrophotometry; D013329:Structure-Activity Relationship; D013696:Temperature; D013816:Thermodynamics
D001426:Bacterial Proteins; D020283:Photoreceptors, Microbial; C050162:photoactive yellow protein, Bacteria