The Supramolecular Architecture of the Bacterial Photosynthetic Apparatus Studied by Atomic Force Microscopy (AFM)
The atomic force microscope (AFM) has developed into a powerful tool in structural biology allowing topographical information of membrane proteins at submolecular resolution to be acquired. Recently, AFM has been demonstrated to be the unique tool to image the photosynthetic apparatus in native membranes from different photosynthetic bacteria species. This chapter provides rationales how to image at high resolution a native membrane using the AFM, and summarizes the recent results concerning the structure and the supramolecular assembly of the photosynthetic complexes. On the single molecule level, membrane proteins directly studied in the native membrane were never subject to extraction, purifi cation, reconstitution, or crystallization. Hence structural data in a native state and information concerning structural heterogeneity of the individual photosynthetic complexes are contributed. On the level of multi-protein assemblies, experimental images of the supramolecular architecture of the photosynthetic apparatus, its adaptation to environmental factors, and its particularities among species are reported.
KeywordsPhotosynthetic Apparatus Rhodobacter Sphaeroides Atomic Force Microscopy Analysis Native Membrane Protein Side Chain
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- Deisenhofer J, Epp O, Miki K, Huber R and Michel H (1984) X- ray structure analysis of a membrane protein complex. Electron density map at 3 Å resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis. J Mol Biol 180: 385-398CrossRefPubMedGoogle Scholar
- Israelachvili J (1991) Intermolecular and Surface Forces. Academic Press, LondonGoogle Scholar
- Scheuring S, Busselez J and Levy D (2005a) Structure of the di- meric PufX-containing core complex of Rhodobacter blasticus by in situ AFM. J Biol Chem 180: 1426-1431Google Scholar