Structural highlights
4i7z is a 8 chain structure with sequence from Mastigocladus laminosus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , , , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
CYB6_MASLA Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.[HAMAP-Rule:MF_00633]
Publication Abstract from PubMed
Cytochrome b6f catalyzes quinone redox reactions within photosynthetic membranes to generate a transmembrane proton electrochemical gradient for ATP synthesis. A key step involves the transfer of an electron from the [2Fe-2S] cluster of the iron-sulfur protein (ISP) extrinsic domain to the cytochrome f heme across a distance of 26 A, which is too large for competent electron transfer but could be bridged by translation-rotation of the ISP. Here we report the first crystallographic evidence of significant motion of the ISP extrinsic domain. It is inferred that extensive crystallographic disorder of the ISP extrinsic domain indicates conformational flexibility. The ISP disorder observed in this structure, in contrast to the largely ordered ISP structure observed in the b6f complex supplemented with neutral lipids, is attributed to electrostatic interactions arising from anionic lipids.
Lipid-induced conformational changes within the cytochrome b6f complex of oxygenic photosynthesis.,Hasan SS, Stofleth JT, Yamashita E, Cramer WA Biochemistry. 2013 Apr 16;52(15):2649-54. doi: 10.1021/bi301638h. Epub 2013 Apr, 5. PMID:23514009[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hasan SS, Stofleth JT, Yamashita E, Cramer WA. Lipid-induced conformational changes within the cytochrome b6f complex of oxygenic photosynthesis. Biochemistry. 2013 Apr 16;52(15):2649-54. doi: 10.1021/bi301638h. Epub 2013 Apr, 5. PMID:23514009 doi:http://dx.doi.org/10.1021/bi301638h
