4V8K
Crystal structure of the LH1-RC complex from Thermochromatium tepidum in P21 form
This is a non-PDB format compatible entry.
Summary for 4V8K
| Entry DOI | 10.2210/pdb4v8k/pdb |
| Related | 3WMM |
| Descriptor | Photosynthetic reaction center cytochrome c subunit, BACTERIOPHEOPHYTIN A, Ubiquinone-8, ... (17 entities in total) |
| Functional Keywords | photosynthesis |
| Biological source | Thermochromatium tepidum More |
| Cellular location | Cellular chromatophore membrane ; Lipid-anchor : D2Z0P5 |
| Total number of polymer chains | 72 |
| Total formula weight | 785238.14 |
| Authors | Niwa, S.,Takeda, K.,Wang-Otomo, Z.-Y.,Miki, K. (deposition date: 2013-11-22, release date: 2014-07-09, Last modification date: 2024-03-20) |
| Primary citation | Niwa, S.,Yu, L.J.,Takeda, K.,Hirano, Y.,Kawakami, T.,Wang-Otomo, Z.Y.,Miki, K. Structure of the LH1-RC complex from Thermochromatium tepidum at 3.0 angstrom Nature, 508:228-232, 2014 Cited by PubMed Abstract: The light-harvesting core antenna (LH1) and the reaction centre (RC) of purple photosynthetic bacteria form a supramolecular complex (LH1-RC) to use sunlight energy in a highly efficient manner. Here we report the first near-atomic structure, to our knowledge, of a LH1-RC complex, namely that of a Ca(2+)-bound complex from Thermochromatium tepidum, which reveals detailed information on the arrangement and interactions of the protein subunits and the cofactors. The RC is surrounded by 16 heterodimers of the LH1 αβ-subunit that form a completely closed structure. The Ca(2+) ions are located at the periplasmic side of LH1. Thirty-two bacteriochlorophyll and 16 spirilloxanthin molecules in the LH1 ring form an elliptical assembly. The geometries of the pigment assembly involved in the absorption characteristics of the bacteriochlorophyll in LH1 and excitation energy transfer among the pigments are reported. In addition, possible ubiquinone channels in the closed LH1 complex are proposed based on the atomic structure. PubMed: 24670637DOI: 10.1038/nature13197 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.006 Å) |
Structure validation
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