TAILIEUCHUNG - Báo cáo khoa học: The single tryptophan of the PsbQ protein of photosystem II is at the end of a 4-a-helical bundle domain

We examined the microenvironment of the single trypto-phan and the tyrosine residues of PsbQ, one of the three main extrinsic proteins of green algal and higher plant photosystem II. On the basis of this information and the previous data on secondary structure [Balsera, M., Arel-lano, ., Gutie´rrez, ., Heredia, P., Revuelta, . & De Las Rivas, J. (2003)Biochemistry42, 1000–1007], we screened structural models derived by combining various threading approaches. | Eur. J. Biochem. 270 3916-3927 2003 FEBS 2003 doi The single tryptophan of the PsbQ protein of photosystem II is at the end of a 4-a-helical bundle domain Monica Balsera1 Juan B. Arellano1 Florencio Pazos2 I Damien Devos2 t Alfonso Valencia2 and Javier De Las Rivas1 1Instituto de Recursos Naturales y Agrobiologia CSIC Cordel de Merinas Salamanca Spain 2Centro National de Biotecnologia CSIC Cantoblanco Madrid Spain We examined the microenvironment of the single tryptophan and the tyrosine residues of PsbQ one of the three main extrinsic proteins of green algal and higher plant photosystem II. On the basis of this information and the previous data on secondary structure Balsera M. Arellano . Gutierrez . Heredia P. Revuelta . De Las Rivas J. 2003 Biochemistry 42 1000-1007 we screened structural models derived by combining various threading approaches. Experimental results showed that the tryptophan residue is partially buried in the core of the protein but still in a polar environment according to the intrinsic fluorescence emission of PsbQ and the fact that fluorescence quenching by iodide was weaker than that by acrylamide. Furthermore quenching by cesium suggested that a positively charged barrier shields the tryptophan microenvironment. Comparison of the absorption spectra in native and denaturing conditions indicated that one or two out of six tyrosines of PsbQ are buried in the core of the structure. Using threading methods a 3D structural model was built for the C-terminal domain of the PsbQ protein family residues 46-149 while the N-terminal domain is predicted to have a flexible structure. The model for the C-terminal domain is based on the 3D structure of cytochrome b562 a mainly a-protein with a helical up down bundle folding. Despite the large sequence differences between the template and PsbQ the structural and energetic parameters for the explicit model are acceptable as judged by the corresponding tools. This 3D

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