Secondary structure of the 33 kDa, extrinsic protein of Photosystem II: a far-UV circular dichroism study

Abstract

The 33 kDa extrinsic protein of Photosystem II is an important component of the oxygen-evolving apparatus which functions to stabilize the manganese cluster at physiological chloride concentrations and to lower the calcium requirement for oxygen evolution. Chou-Fasman analysis of the amino-acid sequence of this protein suggests that this component contains a high proportion of alpha-helical structure and only relatively small amounts of beta-sheet structure. A computational study using more sophisticated techniques (Beauregard, M. (1992) Environ. Exp. Bot. 32, 411-429) concluded that the protein contained little periodically ordered secondary structure. In this study, we have directly measured the relative proportions of secondary structure present in the 33 kDa protein using far-ultraviolet circular dichroism spectroscopy. Our results indicate that, in solution, this protein contains a large proportion of beta-sheet structure (38%) and relatively small amounts of alpha-helical structure (9%). A structural model of the 33 kDa protein based on a constrained Chou-Fasman analysis (Teeter, M.M. and Whitlow, M (1988) Proteins 4, 262-273) is presented.