Backbone assignment and secondary structure of the PsbQ protein from Photosystem II

0372479 - ÚVGZ 2012 RIV DE eng J - Journal Article
Horničáková, M. - Kohoutová, Jaroslava - Schlagnitweit, J. - Wohlschlager, Ch. - Ettrich, Rüdiger - Fiala, R. - Schoefberger, W. - Müller, N.
Backbone assignment and secondary structure of the PsbQ protein from Photosystem II.
Biomolecular NMR Assignments. Roč. 5, č. 2 (2011), s. 169-175. ISSN 1874-2718. E-ISSN 1874-270X
R&D Projects: GA MŠMT(CZ) LC06010
Institutional research plan: CEZ:AV0Z60870520
Keywords : Photosystem II * PsbQ * Missing link * NMR resonance assignment * Protein-protein interaction
Subject RIV: BO - Biophysics
Impact factor: 0.720, year: 2011
http://www.springerlink.com/content/3n38075w5h1l1082/fulltext.pdf

PsbQ is one of the extrinsic proteins situated on the lumenal surface of photosystem II (PSII) in the higher plants and green algae. Its three-dimensional structure was determined by X-ray crystallography with exception of the residues 14-33. To obtain further details about its structure and potentially its dynamics, we approached the problem by NMR. In this paper we report (1)H, (15)N, and (13)C NMR assignments for the PsbQ protein. The very challenging oligo-proline stretches could be assigned using (13)C-detected NMR experiments that enabled the assignments of twelve out of the thirteen proline residues of PsbQ. The identification of PsbQ secondary structure elements on the basis of our NMR data was accomplished with the programs TALOS+, web server CS23D and CS-Rosetta. To obtain additional secondary structure information, three-bond H(N)-H(alpha) J-coupling constants and deviation of experimental (13)C(alpha) and (13)C(beta) chemical shifts from random coil values were determined. The resulting "consensus" secondary structure of PsbQ compares very well with the resolved regions of the published X-ray crystallographic structure and gives a first estimate of the structure of the "missing link" (i.e. residues 14-33), which will serve as the basis for the further investigation of the structure, dynamics and interactions.
Permanent Link: http://hdl.handle.net/11104/0205791