Caffarri Stefano, Passarini Francesca, Bassi Roberto, Croce Roberta
Laboratoire de Génétique et Biophysique des Plante, UMR 6191, CEA-CNRS-Université de la Méditerranée, 163 Av. de Luminy, 13288 Marseille, France.
FEBS Lett. 2007 Oct 2;581(24):4704-10. doi: 10.1016/j.febslet.2007.08.066. Epub 2007 Sep 4.
The location of the neoxanthin binding site in CP26 and CP29 was investigated by site-directed mutagenesis. The crystallographic structure of LHCII shows that the binding of neoxanthin to the N1 site is stabilised by an H bond with a tyrosine in the lumenal loop. This residue is conserved in CP26 and CP29. Mutation of this tyrosine into phenylalanine induced specific loss of neoxanthin without affecting violaxanthin binding. In contrast to previous proposals, it is thus concluded that also in these minor antenna complexes neoxanthin is accommodated in the N1 site. The characteristics of this binding site in the different antenna complexes are discussed.
通过定点诱变研究了新黄质在CP26和CP29中的结合位点位置。LHCII的晶体结构表明,新黄质与N1位点的结合通过与腔环中酪氨酸形成的氢键得以稳定。该残基在CP26和CP29中保守。将此酪氨酸突变为苯丙氨酸会导致新黄质特异性丧失,而不影响紫黄质的结合。与之前的观点相反,因此得出结论,在这些较小的天线复合体中,新黄质也存在于N1位点。讨论了不同天线复合体中该结合位点的特征。