1Q90
Structure of the cytochrome b6f (plastohydroquinone : plastocyanin oxidoreductase) from Chlamydomonas reinhardtii
Summary for 1Q90
| Entry DOI | 10.2210/pdb1q90/pdb |
| Descriptor | Apocytochrome f, HEME C, BETA-CAROTENE, ... (18 entities in total) |
| Functional Keywords | membrane protein complex, photosynthesis, electron transfer, oxydoreductase, chlorophyll, beta-carotene, stigmatellin, sulfoquinovosyldiacylglycerol, monogalactosyldiacylglycerol |
| Biological source | Chlamydomonas reinhardtii More |
| Cellular location | Plastid, chloroplast thylakoid membrane; Single-pass membrane protein: P23577 P49728 P23230 P49728 Q08362 Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein: Q00471 Q42496 Plastid, chloroplast thylakoid membrane; Single-pass membrane protein (By similarity): P50369 P50369 |
| Total number of polymer chains | 9 |
| Total formula weight | 113863.18 |
| Authors | Stroebel, D.,Choquet, Y.,Popot, J.-L.,Picot, D. (deposition date: 2003-08-22, release date: 2003-12-09, Last modification date: 2024-10-30) |
| Primary citation | Stroebel, D.,Choquet, Y.,Popot, J.-L.,Picot, D. An Atypical Haem in the Cytochrome B6F Complex Nature, 426:413-418, 2003 Cited by PubMed Abstract: Photosystems I and II (PSI and II) are reaction centres that capture light energy in order to drive oxygenic photosynthesis; however, they can only do so by interacting with the multisubunit cytochrome b(6)f complex. This complex receives electrons from PSII and passes them to PSI, pumping protons across the membrane and powering the Q-cycle. Unlike the mitochondrial and bacterial homologue cytochrome bc(1), cytochrome b(6)f can switch to a cyclic mode of electron transfer around PSI using an unknown pathway. Here we present the X-ray structure at 3.1 A of cytochrome b(6)f from the alga Chlamydomonas reinhardtii. The structure bears similarities to cytochrome bc(1) but also exhibits some unique features, such as binding chlorophyll, beta-carotene and an unexpected haem sharing a quinone site. This haem is atypical as it is covalently bound by one thioether linkage and has no axial amino acid ligand. This haem may be the missing link in oxygenic photosynthesis. PubMed: 14647374DOI: 10.1038/nature02155 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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