TY - JOUR T1 - A Novel Membrane Protein in the <em>Rhodobacter sphaeroides</em> LH1-RC Photocomplex JF - bioRxiv DO - 10.1101/2021.06.20.449127 SP - 2021.06.20.449127 AU - K. Tani AU - K. V. P. Nagashima AU - R. Kanno AU - S. Kawamura AU - R. Kikuchi AU - M. Hall AU - L.-J. Yu AU - Y. Kimura AU - M. T. Madigan AU - A. Mizoguchi AU - B. M. Humbel AU - Z.-Y. Wang-Otomo Y1 - 2021/01/01 UR - http://biorxiv.org/content/early/2021/06/20/2021.06.20.449127.abstract N2 - We present a cryo-EM structure of the monomeric light-harvesting-reaction center (LH1-RC) core complex from photosynthetic purple bacterium Rhodobacter (Rba.) sphaeroides at 2.9 Å resolution. The LH1 complex forms a C-shaped structure composed of 14 αβ-polypeptides around the RC with a large ring opening. From the cryo-EM density map, a previously unrecognized integral membrane protein, referred to as protein-U, was identified. Protein-U has a U-shaped conformation near the LH1-ring opening and was annotated as a hypothetical protein in the Rba. sphaeroides genome. Deletion of protein-U resulted in a mutant strain that expressed a much-reduced amount of the dimeric LH1-RC, indicating an important role for protein-U in dimerization of the LH1-RC complex. PufX was located opposite protein-U on the LH1-ring opening, and both its position and conformation differed from that of previous reports of dimeric LH1-RC structures obtained at low-resolution. Twenty-six molecules of the carotenoid spheroidene arranged in two distinct configurations were resolved in the Rba. sphaeroides LH1 and were positioned within the complex to block its pores. Our findings offer a new view of the core photocomplex of Rba. sphaeroides and the connections between structure and function in bacterial photocomplexes in general.Competing Interest StatementThe authors have declared no competing interest. ER -