Crystal structures of two camelid nanobodies raised against GldL, a component of the type IX secretion system from Flavobacterium johnsoniae. Issue 6 (24th May 2021)

• Record Type: Journal Article
• Authors: Trinh, Thi Trang Nhung; Gaubert, Anaïs; Melani, Pauline; Cambillau, Christian; Roussel, Alain; Leone, Philippe
• Is Part Of: Acta crystallographica. Volume 77:Issue 6(2021)
• Page Start: 171
• Page End: 176
• Publication Date: 2021-05-24
• Subjects: camelid nanobodies -- type IX secretion system -- Flavobacterium johnsoniae -- GldL interaction -- crystallization chaperones -- domain swapping; Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X21005185
• Languages: English
• ISSNs: 2053-230X

Abstract

Abstract : Two nanobodies raised against the cytoplasmic domain of GldL were produced, their interaction with their target was characterized, and their crystal structures were solved. Abstract : 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.