Solution NMR and molecular dynamics reveal a persistent alpha helix within the dynamic region of PsbQ from photosystem II of higher plants

0472747 - MBÚ 2017 RIV US eng J - Článek v odborném periodiku
Rathner, P. - Rathner, A. - Horničáková, M. - Wohlschlager, Ch. - Chandra, K. - Kohoutová, Jaroslava - Ettrich, Rüdiger - Wimmer, R. - Müller, N.
Solution NMR and molecular dynamics reveal a persistent alpha helix within the dynamic region of PsbQ from photosystem II of higher plants.
Proteins-Structure, Function and Bioinformatics. Roč. 83, č. 9 (2015), s. 1677-1686. ISSN 0887-3585. E-ISSN 1097-0134
Institucionální podpora: RVO:61388971
Klíčová slova: dynamic N-terminus * extrinsic photosynthetic protein * hydrogen bond dynamics
Kód oboru RIV: EE - Mikrobiologie, virologie
Impakt faktor: 2.499, rok: 2015

The extrinsic proteins of photosystem II of higher plants and green algae PsbO, PsbP, PsbQ, and PsbR are essential for stable oxygen production in the oxygen evolving center. In the available X-ray crystallographic structure of higher plant PsbQ residues S14-Y33 are missing. Building on the backbone NMR assignment of PsbQ, which includes this missing link, we report the extended resonance assignment including side chain atoms. Based on nuclear Overhauser effect spectra a high resolution solution structure of PsbQ with a backbone RMSD of 0.81 angstrom was obtained from torsion angle dynamics. Within the N-terminal residues 1-45 the solution structure deviates significantly from the X-ray crystallographic one, while the four-helix bundle core found previously is confirmed. A short -helix is observed in the solution structure at the location where a -strand had been proposed in the earlier crystallographic study. NMR relaxation data and unrestrained molecular dynamics simulations corroborate that the N-terminal region behaves as a flexible tail with a persistent short local helical secondary structure, while no indications of forming a -strand are found. Proteins 2015; 83:1677-1686. (c) 2015 The Authors. Proteins: Structure, Function, and Bioinformatics
Trvalý link: http://hdl.handle.net/11104/0269979