8fb9 | pdb_00008fb9

LH2-LH3 antenna in anti parallel configuration embedded in a nanodisc

spinqualitylabelsall models 8fb9, resolution 6.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8fb9 is a 32 chain structure with sequence from Magnetospirillum molischianum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 6.4Å Ligands: BCL, LYC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q7M119_MAGML Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.[ARBA:ARBA00002455] Publication Abstract from PubMed In photosynthesis, absorbed light energy transfers through a network of antenna proteins with near-unity quantum efficiency to reach the reaction center, which initiates the downstream biochemical reactions. While the energy transfer dynamics within individual antenna proteins have been extensively studied over the past decades, the dynamics between the proteins are poorly understood due to the heterogeneous organization of the network. Previously reported timescales averaged over such heterogeneity, obscuring individual interprotein energy transfer steps. Here, we isolated and interrogated interprotein energy transfer by embedding two variants of the primary antenna protein from purple bacteria, light-harvesting complex 2 (LH2), together into a near-native membrane disc, known as a nanodisc. We integrated ultrafast transient absorption spectroscopy, quantum dynamics simulations, and cryogenic electron microscopy to determine interprotein energy transfer timescales. By varying the diameter of the nanodiscs, we replicated a range of distances between the proteins. The closest distance possible between neighboring LH2, which is the most common in native membranes, is 25 A and resulted in a timescale of 5.7 ps. Larger distances of 28 to 31 A resulted in timescales of 10 to 14 ps. Corresponding simulations showed that the fast energy transfer steps between closely spaced LH2 increase transport distances by approximately 15%. Overall, our results introduce a framework for well-controlled studies of interprotein energy transfer dynamics and suggest that protein pairs serve as the primary pathway for the efficient transport of solar energy. Elucidating interprotein energy transfer dynamics within the antenna network from purple bacteria.,Wang D, Fiebig OC, Harris D, Toporik H, Ji Y, Chuang C, Nairat M, Tong AL, Ogren JI, Hart SM, Cao J, Sturgis JN, Mazor Y, Schlau-Cohen GS Proc Natl Acad Sci U S A. 2023 Jul 11;120(28):e2220477120. doi: , 10.1073/pnas.2220477120. Epub 2023 Jul 3. PMID:37399405 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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