6S2Z
Water-soluble Chlorophyll Protein (WSCP) from Brassica oleracea var. Botrytis with Chlorophyll-b
Summary for 6S2Z
| Entry DOI | 10.2210/pdb6s2z/pdb |
| Descriptor | Water-Soluble Chlorophyll Protein, CHLOROPHYLL B (3 entities in total) |
| Functional Keywords | tetramer, plant, brassica oleracea, chlorophyll, water-soluble chlorophyll protein, photooxidation, chlorophyll carrier, plant protein |
| Biological source | Brassica oleracea var. botrytis (Cauliflower) |
| Total number of polymer chains | 1 |
| Total formula weight | 20079.20 |
| Authors | Agostini, A.,Meneghin, E.,Gewehr, L.,Pedron, D.,Palm, D.M.,Carbonera, D.,Paulsen, H.,Jaenicke, E.,Collini, E. (deposition date: 2019-06-23, release date: 2019-12-18, Last modification date: 2024-10-09) |
| Primary citation | Agostini, A.,Meneghin, E.,Gewehr, L.,Pedron, D.,Palm, D.M.,Carbonera, D.,Paulsen, H.,Jaenicke, E.,Collini, E. How water-mediated hydrogen bonds affect chlorophyll a/b selectivity in Water-Soluble Chlorophyll Protein. Sci Rep, 9:18255-18255, 2019 Cited by PubMed Abstract: The Water-Soluble Chlorophyll Protein (WSCP) of Brassicaceae is a remarkably stable tetrapyrrole-binding protein that, by virtue of its simple design, is an exceptional model to investigate the interactions taking place between pigments and their protein scaffold and how they affect the photophysical properties and the functionality of the complexes. We investigated variants of WSCP from Lepidium virginicum (Lv) and Brassica oleracea (Bo), reconstituted with Chlorophyll (Chl) b, to determine the mechanisms by which the different Chl binding sites control their Chl a/b specificities. A combined Raman and crystallographic investigation has been employed, aimed to characterize in detail the hydrogen-bond network involving the formyl group of Chl b. The study revealed a variable degree of conformational freedom of the hydrogen bond networks among the WSCP variants, and an unexpected mixed presence of hydrogen-bonded and not hydrogen-bonded Chls b in the case of the L91P mutant of Lv WSCP. These findings helped to refine the description of the mechanisms underlying the different Chl a/b specificities of WSCP versions, highlighting the importance of the structural rigidity of the Chl binding site in the vicinity of the Chl b formyl group in granting a strong selectivity to binding sites. PubMed: 31796824DOI: 10.1038/s41598-019-54520-4 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
Download full validation report
