Origins of the Intermediate Spectral Form in M100 Mutants of Photoactive Yellow Protein.

ABSTRACT: Numerous single-site mutants of photoactive yellow protein (PYP) from Halorhodospira halophila and as well as PYP homologs from other species exhibit a shoulder on the short wavelength side of the absorbance maximum in their dark-adapted states. The structural basis for the occurrence of this shoulder, called the "intermediate spectral form," has only been investigated in detail for the Y42F mutation. Here we explore the structural basis for occurrence of the intermediate spectral form in a M121E derivative of a circularly permuted H. halophila PYP (M121E-cPYP). The M121 site in M121E-cPYP corresponds to the M100 site in wild-type H. halophila PYP. High-resolution NMR measurements with a salt-tolerant cryoprobe enabled identification of those residues directly affected by increasing concen

SUBMITTER: Kumar A 

PROVIDER: S-EPMC4489994 | biostudies-literature | 2015 Jul-Aug

REPOSITORIES: biostudies-literature