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Structure paper

TitleHigh-resolution structure and biochemical properties of the LH1-RC photocomplex from the model purple sulfur bacterium, Allochromatium vinosum.
Journal, issue, pagesCommun Biol, Vol. 7, Issue 1, Page 176, Year 2024
Publish dateFeb 12, 2024
AuthorsKazutoshi Tani / Ryo Kanno / Ayaka Harada / Yuki Kobayashi / Akane Minamino / Shinji Takenaka / Natsuki Nakamura / Xuan-Cheng Ji / Endang R Purba / Malgorzata Hall / Long-Jiang Yu / Michael T Madigan / Akira Mizoguchi / Kenji Iwasaki / Bruno M Humbel / Yukihiro Kimura / Zheng-Yu Wang-Otomo /
PubMed AbstractThe mesophilic purple sulfur phototrophic bacterium Allochromatium (Alc.) vinosum (bacterial family Chromatiaceae) has been a favored model for studies of bacterial photosynthesis and sulfur ...The mesophilic purple sulfur phototrophic bacterium Allochromatium (Alc.) vinosum (bacterial family Chromatiaceae) has been a favored model for studies of bacterial photosynthesis and sulfur metabolism, and its core light-harvesting (LH1) complex has been a focus of numerous studies of photosynthetic light reactions. However, despite intense efforts, no high-resolution structure and thorough biochemical analysis of the Alc. vinosum LH1 complex have been reported. Here we present cryo-EM structures of the Alc. vinosum LH1 complex associated with reaction center (RC) at 2.24 Å resolution. The overall structure of the Alc. vinosum LH1 resembles that of its moderately thermophilic relative Alc. tepidum in that it contains multiple pigment-binding α- and β-polypeptides. Unexpectedly, however, six Ca ions were identified in the Alc. vinosum LH1 bound to certain α1/β1- or α1/β3-polypeptides through a different Ca-binding motif from that seen in Alc. tepidum and other Chromatiaceae that contain Ca-bound LH1 complexes. Two water molecules were identified as additional Ca-coordinating ligands. Based on these results, we reexamined biochemical and spectroscopic properties of the Alc. vinosum LH1-RC. While modest but distinct effects of Ca were detected in the absorption spectrum of the Alc. vinosum LH1 complex, a marked decrease in thermostability of its LH1-RC complex was observed upon removal of Ca. The presence of Ca in the photocomplex of Alc. vinosum suggests that Ca-binding to LH1 complexes may be a common adaptation in species of Chromatiaceae for conferring spectral and thermal flexibility on this key component of their photosynthetic machinery.
External linksCommun Biol / PubMed:38347078 / PubMed Central
MethodsEM (single particle)
Resolution2.24 Å
Structure data

37465

8wdu

EMDB-37465, PDB-8wdu:
Photosynthetic LH1-RC complex from the purple sulfur bacterium Allochromatium vinosum purified by sucrose density
Method: EM (single particle) / Resolution: 2.24 Å

37466

8wdv

EMDB-37466, PDB-8wdv:
Photosynthetic LH1-RC complex from the purple sulfur bacterium Allochromatium vinosum purified by Ca2+-DEAE
Method: EM (single particle) / Resolution: 2.24 Å

Chemicals

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE / Heme B

ChemComp-MG:
Unknown entry

ChemComp-Z41:
(2S)-3-hydroxypropane-1,2-diyl dihexadecanoate

ChemComp-PLM:
PALMITIC ACID / Palmitic acid

ChemComp-PGV:
(1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE / phospholipid*YM / Phosphatidylglycerol

ChemComp-BCL:
BACTERIOCHLOROPHYLL A / Bacteriochlorophyll

ChemComp-BPH:
BACTERIOPHEOPHYTIN A / Pheophytin

ChemComp-UQ8:
Ubiquinone-8

ChemComp-LMT:
DODECYL-BETA-D-MALTOSIDE / detergent*YM

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM / Cardiolipin

ChemComp-FE:
Unknown entry / Iron

ChemComp-MQ8:
MENAQUINONE 8 / Vitamin K2

ChemComp-CRT:
SPIRILLOXANTHIN

ChemComp-CA:
Unknown entry

ChemComp-LDA:
LAURYL DIMETHYLAMINE-N-OXIDE / LDAO, detergent*YM / Lauryldimethylamine oxide

ChemComp-HOH:
WATER / Water

Source
  • allochromatium vinosum dsm 180 (bacteria)
KeywordsPHOTOSYNTHESIS / LH1-RC COMPLEX / PURPLE SULFUR BACTERIA

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