Use of protein cross-linking and radiolytic labeling to elucidate the structure of PsbO within higher-plant photosystem II

TitleUse of protein cross-linking and radiolytic labeling to elucidate the structure of PsbO within higher-plant photosystem II
Publication TypeJournal Article
Year of Publication2016
AuthorsMummadisetti MP, Frankel LK, Bellamy HD, Sallans L, Goettert JS, Brylinski M, Bricker TM
JournalBiochemistry
Volume55
Issue23
Pagination3204-13
Date Published2016 Jun 14
ISSN1520-4995
Abstract

We have used protein cross-linking with the zero-length cross-linker 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide, and radiolytic footprinting coupled with high-resolution tandem mass spectrometry, to examine the structure of higher-plant PsbO when it is bound to Photosystem II. Twenty intramolecular cross-linked residue pairs were identified. On the basis of this cross-linking data, spinach PsbO was modeled using the Thermosynechococcus vulcanus PsbO structure as a template, with the cross-linking distance constraints incorporated using the MODELLER program. Our model of higher-plant PsbO identifies several differences between the spinach and cyanobacterial proteins. The N-terminal region is particularly interesting, as this region has been suggested to be important for oxygen evolution and for the specific binding of PsbO to Photosystem II. Additionally, using radiolytic mapping, we have identified regions on spinach PsbO that are shielded from the bulk solvent. These domains may represent regions on PsbO that interact with other components, as yet unidentified, of the photosystem.

DOI10.1021/acs.biochem.6b00365
Alternate JournalBiochemistry
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