Structural highlights
Publication Abstract from PubMed
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.
Crystal structures of two camelid nanobodies raised against GldL, a component of the type IX secretion system from Flavobacterium johnsoniae.,Trinh TTN, Gaubert A, Melani P, Cambillau C, Roussel A, Leone P Acta Crystallogr F Struct Biol Commun. 2021 Jun 1;77(Pt 6):171-176. doi:, 10.1107/S2053230X21005185. Epub 2021 May 24. PMID:34100775[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Trinh TTN, Gaubert A, Melani P, Cambillau C, Roussel A, Leone P. Crystal structures of two camelid nanobodies raised against GldL, a component of the type IX secretion system from Flavobacterium johnsoniae. Acta Crystallogr F Struct Biol Commun. 2021 Jun 1;77(Pt 6):171-176. doi:, 10.1107/S2053230X21005185. Epub 2021 May 24. PMID:34100775 doi:http://dx.doi.org/10.1107/S2053230X21005185
