6gix

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

spinqualitylabelsall models 6gix, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6gix is a 4 chain structure with sequence from Lepidium virginicum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function O04797_LEPVR 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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