A Ca²⁺-binding motif underlies the unusual properties of certain photosynthetic bacterial core light-harvesting complexes.

ABSTRACT: The mildly thermophilic purple phototrophic bacterium Allochromatium tepidum provides a unique model for investigating various intermediate phenotypes observed between those of thermophilic and mesophilic counterparts. The core light-harvesting (LH1) complex from A. tepidum exhibits an absorption maximum at 890 nm and mildly enhanced thermostability, both of which are Ca²⁺-dependent. However, it is unknown what structural determinants might contribute to these properties. Here, we present a cryo-EM structure of the reaction center-associated LH1 complex at 2.81 Å resolution, in which we identify multiple pigment-binding α- and β-polypeptides within an LH1 ring. Of the 16 α-polypeptides, we show that six (α1) bind Ca²⁺ along with β1- or β3-polypeptides to form the Ca

SUBMITTER: Tani K 

PROVIDER: S-EPMC9133646 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature