1IJD
Crystallographic Structure of the LH3 Complex from Rhodopseudomonas acidophila strain 7050
Summary for 1IJD
| Entry DOI | 10.2210/pdb1ijd/pdb |
| Related | 1KZU 1LGH |
| Descriptor | LIGHT-HARVESTING PROTEIN B-800/820, ALPHA CHAIN, LIGHT-HARVESTING PROTEIN B-800/820, BETA CHAIN, BACTERIOCHLOROPHYLL A, ... (6 entities in total) |
| Functional Keywords | pigment-protein complex, alpha-helix apoproteins, intergral membrane protein, light harvesting, photosynthesis |
| Biological source | Rhodoblastus acidophilus More |
| Cellular location | Cell inner membrane; Single-pass type II membrane protein: P35089 P35094 |
| Total number of polymer chains | 6 |
| Total formula weight | 42203.99 |
| Authors | McLuskey, K.,Prince, S.M.,Cogdell, R.J.,Isaacs, N.W. (deposition date: 2001-04-25, release date: 2001-10-17, Last modification date: 2024-11-06) |
| Primary citation | McLuskey, K.,Prince, S.M.,Cogdell, R.J.,Isaacs, N.W. The crystallographic structure of the B800-820 LH3 light-harvesting complex from the purple bacteria Rhodopseudomonas acidophila strain 7050. Biochemistry, 40:8783-8789, 2001 Cited by PubMed Abstract: The B800-820, or LH3, complex is a spectroscopic variant of the B800-850 LH2 peripheral light-harvesting complex. LH3 is synthesized by some species and strains of purple bacteria when growing under what are generally classed as "stressed" conditions, such as low intensity illumination and/or low temperature (<30 degrees C). The apoproteins in these complexes modify the absorption properties of the chromophores to ensure that the photosynthetic process is highly efficient. The crystal structure of the B800-820 light-harvesting complex, an integral membrane pigment-protein complex, from the purple bacteria Rhodopseudomonas (Rps.) acidophila strain 7050 has been determined to a resolution of 3.0 A by molecular replacement. The overall structure of the LH3 complex is analogous to that of the LH2 complex from Rps. acidophila strain 10050. LH3 has a nonameric quaternary structure where two concentric cylinders of alpha-helices enclose the pigment molecules bacteriochlorophyll a and carotenoid. The observed spectroscopic differences between LH2 and LH3 can be attributed to differences in the primary structure of the apoproteins. There are changes in hydrogen bonding patterns between the coupled Bchla molecules and the protein that have an effect on the conformation of the C3-acetyl groups of the B820 molecules. The structure of LH3 shows the important role that the protein plays in modulating the characteristics of the light-harvesting system and indicates the mechanisms by which the absorption properties of the complex are altered to produce a more efficient light-harvesting component. PubMed: 11467938DOI: 10.1021/bi010309a PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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