Crystal structure of the Psb27 assembly factor at 1.6: implications for binding to Photosystem II

0388577 - MBÚ 2013 RIV NL eng J - Článek v odborném periodiku
Michoux, F. - Takasaka, K. - Boehm, M. - Komenda, Josef - Nixon, P. J. - Murray, J. W.
Crystal structure of the Psb27 assembly factor at 1.6: implications for binding to Photosystem II.
Photosynthesis Research. Roč. 110, č. 3 (2012), s. 169-175. ISSN 0166-8595. E-ISSN 1573-5079
Grant CEP: GA ČR(CZ) GAP501/11/0377; GA MŠMT(CZ) ED2.1.00/03.0110
Institucionální podpora: RVO:61388971
Klíčová slova: Monomeric and dimeric photosystem II * Assembly * Repair
Kód oboru RIV: EE - Mikrobiologie, virologie
Impakt faktor: 3.150, rok: 2012

The biogenesis and oxygen-evolving activity of cyanobacterial Photosystem II (PSII) is dependent on a number of accessory proteins not found in the crystallised dimeric complex. These include Psb27, a small lipoprotein attached to the lumenal side of PSII, which has been assigned a role in regulating the assembly of the Mn(4)Ca cluster catalysing water oxidation. To gain a better understanding of Psb27, we have determined in this study the crystal structure of the soluble domain of Psb27 from Thermosynechococcus elongatus to a resolution of 1.6 . The structure is a four-helix bundle, similar to the recently published solution structures of Psb27 from Synechocystis PCC 6803 obtained by nuclear magnetic resonance (NMR) spectroscopy. Importantly, the crystal structure presented here helps us resolve the differences between the NMR-derived structural models. Potential binding sites for Psb27 within PSII are discussed in light of recent biochemical data in the literature
Trvalý link: http://hdl.handle.net/11104/0217470