6GIW

Water-soluble Chlorophyll Protein (WSCP) from Lepidium virginicum (Mutation L91P) with Chlorophyll-a

Summary for 6GIW

• Entry DOI: 10.2210/pdb6giw/pdb
• Descriptor: Water-soluble chlorophyll protein, CHLOROPHYLL A (3 entities in total)
• Functional Keywords: tetramer, plant, lepidium virginicum, chlorophyll, water-soluble chlorophyll protein, photooxidation, chlorophyll carrier, plant protein
• Biological source: Lepidium virginicum
• Total number of polymer chains: 4
• Total formula weight: 81875.89

Authors

Palm, D.M.,Agostini, A.,Averesch, V.,Girr, P.,Werwie, M.,Takahashi, S.,Satoh, H.,Jaenicke, E.,Paulsen, H. (deposition date: 2018-05-15, release date: 2018-10-17, Last modification date: 2024-11-13)

Primary citation

Palm, D.M.,Agostini, A.,Averesch, V.,Girr, P.,Werwie, M.,Takahashi, S.,Satoh, H.,Jaenicke, E.,Paulsen, H.
Chlorophyll a/b binding-specificity in water-soluble chlorophyll protein.
Nat Plants, 4:920-929, 2018

PubMed Abstract: We altered the chlorophyll (Chl) binding sites in various versions of water-soluble chlorophyll protein (WSCP) by amino acid exchanges to alter their preferences for either Chl a or Chl b. WSCP is ideally suited for this mutational analysis since it forms a tetrameric complex with only four identical Chl binding sites. A loop of 4-6 amino acids is responsible for Chl a versus Chl b selectivity. We show that a single amino acid exchange within this loop changes the relative Chl a/b affinities by a factor of 40. We obtained crystal structures of this WSCP variant binding either Chl a or Chl b. The Chl binding sites in these structures were compared with those in the major light-harvesting complex (LHCII) of the photosynthetic apparatus in plants to search for similar structural features involved in Chl a/b binding specificity.

PubMed: 30297830
DOI: 10.1038/s41477-018-0273-z

Experimental method

X-RAY DIFFRACTION (2.8 Å)