Structural highlights
Publication Abstract from PubMed
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.
Chlorophyll a/b binding-specificity in water-soluble chlorophyll protein.,Palm DM, Agostini A, Averesch V, Girr P, Werwie M, Takahashi S, Satoh H, Jaenicke E, Paulsen H Nat Plants. 2018 Oct 8. pii: 10.1038/s41477-018-0273-z. doi:, 10.1038/s41477-018-0273-z. PMID:30297830[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Palm DM, 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. 2018 Oct 8. pii: 10.1038/s41477-018-0273-z. doi:, 10.1038/s41477-018-0273-z. PMID:30297830 doi:http://dx.doi.org/10.1038/s41477-018-0273-z
