Crystal structures of two camelid nanobodies raised against GldL, a component of the type IX secretion system from Flavobacterium johnsoniae

GldL is an inner-membrane protein that is essential for the function of the type IX secretion system (T9SS) in Flavobacterium johnsoniae. The complex that it forms with GldM is supposed to act as a new rotary motor involved in the gliding motility of the bacterium. In the context of structural studi...

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Tác giả chính: T. T. N. Trinh, A. Gaubert, P. Melani, C. Cambillau, A. Roussel, P. Leone
Định dạng: Bài trích
Ngôn ngữ:eng
Nhà xuất bản: Acta Crystallographica Section F 2021
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Truy cập trực tuyến:https://scripts.iucr.org/cgi-bin/paper?S2053230X21005185
https://dlib.phenikaa-uni.edu.vn/handle/PNK/2816
https://doi.org/10.1107/S2053230X21005185
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Tóm tắt:GldL is an inner-membrane protein that is essential for the function of the type IX secretion system (T9SS) in Flavobacterium johnsoniae. The complex that it forms with GldM is supposed to act as a new rotary motor involved in the gliding motility of the bacterium. In the context of structural studies of GldL to gain information on the assembly and function of the T9SS, two camelid nanobodies were selected, produced and purified. Their interaction with the cytoplasmic domain of GldL was characterized and their crystal structures were solved. These nanobodies will be used as crystallization chaperones to help in the crystallization of the cytoplasmic domain of GldL and could also help to solve the structure of the complex using molecular replacement.