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Cryo-EM structures of light-harvesting 2 complexes from Rhodopseudomonas palustris reveal the molecular origin of absorption tuning.


ABSTRACT: The genomes of some purple photosynthetic bacteria contain a multigene puc family encoding a series of α- and β-polypeptides that together form a heterogeneous antenna of light-harvesting 2 (LH2) complexes. To unravel this complexity, we generated four sets of puc deletion mutants in Rhodopseudomonas palustris, each encoding a single type of pucBA gene pair and enabling the purification of complexes designated as PucA-LH2, PucB-LH2, PucD-LH2, and PucE-LH2. The structures of all four purified LH2 complexes were determined by cryogenic electron microscopy (cryo-EM) at resolutions ranging from 2.7 to 3.6 Å. Uniquely, each of these complexes contains a hitherto unknown polypeptide, γ, that forms an extended undulating ribbon that lies in the plane of the membrane and that encloses six of the nine LH2 αβ-subunits. The γ-subunit, which is located near to the cytoplasmic side of the complex, breaks the C9 symmetry of the LH2 complex and binds six extra bacteriochlorophylls (BChls) that enhance the 800-nm absorption of each complex. The structures show that all four complexes have two complete rings of BChls, conferring absorption bands centered at 800 and 850 nm on the PucA-LH2, PucB-LH2, and PucE-LH2 complexes, but, unusually, the PucD-LH2 antenna has only a single strong near-infared (NIR) absorption peak at 803 nm. Comparison of the cryo-EM structures of these LH2 complexes reveals altered patterns of hydrogen bonds between LH2 αβ-side chains and the bacteriochlorin rings, further emphasizing the major role that H bonds play in spectral tuning of bacterial antenna complexes.

SUBMITTER: Qian P 

PROVIDER: S-EPMC9618040 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature

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Cryo-EM structures of light-harvesting 2 complexes from <i>Rhodopseudomonas palustris</i> reveal the molecular origin of absorption tuning.

Qian Pu P   Nguyen-Phan Cam T CT   Gardiner Alastair T AT   Croll Tristan I TI   Roszak Aleksander W AW   Southall June J   Jackson Philip J PJ   Vasilev Cvetelin C   Castro-Hartmann Pablo P   Sader Kasim K   Hunter C Neil CN   Cogdell Richard J RJ  

Proceedings of the National Academy of Sciences of the United States of America 20221017 43


The genomes of some purple photosynthetic bacteria contain a multigene <i>puc</i> family encoding a series of α- and β-polypeptides that together form a heterogeneous antenna of light-harvesting 2 (LH2) complexes. To unravel this complexity, we generated four sets of <i>puc</i> deletion mutants in <i>Rhodopseudomonas palustris</i>, each encoding a single type of <i>pucBA</i> gene pair and enabling the purification of complexes designated as PucA-LH2, PucB-LH2, PucD-LH2, and PucE-LH2. The structu  ...[more]

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