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3BSD

Light harvesting protein from RC of Chlorobium tepidum

Summary for 3BSD
Entry DOI10.2210/pdb3bsd/pdb
DescriptorBacteriochlorophyll a protein, MAGNESIUM ION, BACTERIOCHLOROPHYLL A, ... (4 entities in total)
Functional Keywordsgreen bacteria, photosynthesis, light harvesting, bacteriochlorophyll, chlorophyll, chromophore, electron transport, magnesium, metal-binding, reaction center, transport
Biological sourceChlorobaculum tepidum
Total number of polymer chains1
Total formula weight47659.77
Authors
Nelson, N.,Frolow, F.,Brn-Shem, A. (deposition date: 2007-12-23, release date: 2008-01-22, Last modification date: 2023-11-01)
Primary citationBen-Shem, A.,Frolow, F.,Nelson, N.
Evolution of photosystem I - from symmetry through pseudo-symmetry to asymmetry.
Febs Lett., 564:274-280, 2004
Cited by
PubMed Abstract: The evolution of photosystem (PS) I was probably initiated by the formation of a homodimeric reaction center similar to the one currently present in green bacteria. Gene duplication has generated a heterodimeric reaction center that subsequently evolved to the PSI present in cyanobacteria, algae and plant chloroplasts. During the evolution of PSI several attempts to maximize the efficiency of light harvesting took place in the various organisms. In the Chlorobiaceae, chlorosomes and FMO were added to the homodimeric reaction center. In cyanobacteria phycobilisomes and CP43' evolved to cope with the light limitations and stress conditions. The plant PSI utilizes a modular arrangement of membrane light-harvesting proteins (LHCI). We obtained structural information from the two ends of the evolutionary spectrum. Novel features in the structure of Chlorobium tepidum FMO are reported in this communication. Our structure of plant PSI reveals that the addition of subunit G provided the template for LHCI binding, and the addition of subunit H prevented the possibility of trimer formation and provided a binding site for LHCII and the onset of energy spillover from PSII to PSI.
PubMed: 15111109
DOI: 10.1016/S0014-5793(04)00360-6
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

237735

건을2025-06-18부터공개중

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