5HPZ

type II water soluble Chl binding proteins

Summary for 5HPZ

• Entry DOI: 10.2210/pdb5hpz/pdb
• Descriptor: Water-soluble chlorophyll protein, 13'2-hydroxyl-Chlorophyll a (3 entities in total)
• Functional Keywords: chl spectra in the type ii water soluble chl binding proteins from brassicaceae, chlorophyll binding protein
• Biological source: Brassicaceae (Mustard family); More
• Total number of polymer chains: 2
• Total formula weight: 40106.33

Authors

Bednarczyk, D.,Dym, O.,Prabahard, V.,Noy, D. (deposition date: 2016-01-21, release date: 2016-05-04, Last modification date: 2024-10-23)

Primary citation

Bednarczyk, D.,Dym, O.,Prabahar, V.,Peleg, Y.,Pike, D.H.,Noy, D.
Fine Tuning of Chlorophyll Spectra by Protein-Induced Ring Deformation.
Angew.Chem.Int.Ed.Engl., 55:6901-6905, 2016

PubMed Abstract: The ability to tune the light-absorption properties of chlorophylls by their protein environment is the key to the robustness and high efficiency of photosynthetic light-harvesting proteins. Unfortunately, the intricacy of the natural complexes makes it very difficult to identify and isolate specific protein-pigment interactions that underlie the spectral-tuning mechanisms. Herein we identify and demonstrate the tuning mechanism of chlorophyll spectra in type II water-soluble chlorophyll binding proteins from Brassicaceae (WSCPs). By comparing the molecular structures of two natural WSCPs we correlate a shift in the chlorophyll red absorption band with deformation of its tetrapyrrole macrocycle that is induced by changing the position of a nearby tryptophan residue. We show by a set of reciprocal point mutations that this change accounts for up to 2/3 of the observed spectral shift between the two natural variants.

PubMed: 27098554
DOI: 10.1002/anie.201512001

Experimental method

X-RAY DIFFRACTION (1.96 Å)