Journal
EMBO REPORTS
Volume 4, Issue 9, Pages 900-905Publisher
WILEY
DOI: 10.1038/sj.embor.embor923
Keywords
-
Categories
Ask authors/readers for more resources
The smallest extrinsic polypeptide of the water-oxidizing complex (PsbQ) was extracted and purified from spinach ( Spinacia oleracea) photosystem II ( PSII) membranes. It was then crystallized in the presence of Zn2+ and its structure was determined by X-ray diffraction at 1.95-Angstrom resolution using the multiwavelength anomalous diffraction method, with the zinc as the anomalous scatterer. The crystal structure shows that the core of the protein is a four-helix bundle, whereas the amino-terminal portion, which possibly interacts with the photosystem core, is not visible in the crystal. The distribution of positive and negative charges on the protein surface might explain the ability of PsbQ to increase the binding of Cl- and Ca2+ and make them available to PSII.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available