Scheuring, S. and Reiss-Husson, F. and Engel, A. and Rigaud, J. L. and Ranck, J. L.. (2001) High-resolution AFM topographs of Rubrivivax gelatinosus light-harvesting complex LH2. The EMBO journal, Vol. 20, H. 12. pp. 3029-3035.
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Official URL: http://edoc.unibas.ch/dok/A5257657
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Abstract
Light-harvesting complexes 2 (LH2) are the accessory antenna proteins in the bacterial photosynthetic apparatus and are built up of alphabeta-heterodimers containing three bacteriochlorophylls and one carotenoid each. We have used atomic force microscopy (AFM) to investigate reconstituted LH2 from Rubrivivax gelatinosus, which has a C-terminal hydrophobic extension of 21 amino acids on the alpha-subunit. High-resolution topographs revealed a nonameric organization of the regularly packed cylindrical complexes incorporated into the membrane in both orientations. Native LH2 showed one surface which protruded by approximately 6 A and one that protruded by approximately 14 A from the membrane. Topographs of samples reconstituted with thermolysin-digested LH2 revealed a height reduction of the strongly protruding surface to approximately 9 A, and a change of its surface appearance. These results suggested that the alpha-subunit of R.gelatinosus comprises a single transmembrane helix and an extrinsic C-terminus, and allowed the periplasmic surface to be assigned. Occasionally, large rings ( approximately 120 A diameter) surrounded by LH2 rings were observed. Their diameter and appearance suggest the large rings to be LH1 complexes.
Faculties and Departments: | 05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Structural Biology (Engel) |
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UniBasel Contributors: | Engel, Andreas H |
Item Type: | Article, refereed |
Article Subtype: | Research Article |
Publisher: | Nature Publishing Group |
ISSN: | 0261-4189 |
Note: | Publication type according to Uni Basel Research Database: Journal article |
Last Modified: | 22 Mar 2012 14:20 |
Deposited On: | 22 Mar 2012 13:18 |
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