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Crystal structures of two camelid nanobodies raised against GldL, a component of the type IX secretion system from Flavobacterium johnsoniae
Author(s) -
Trinh Thi Trang Nhung,
Gaubert Anaïs,
Melani Pauline,
Cambillau Christian,
Roussel Alain,
Leone Philippe
Publication year - 2021
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x21005185
Subject(s) - secretion , context (archaeology) , cytoplasm , microbiology and biotechnology , motility , crystallization , biology , chemistry , biochemistry , paleontology , organic chemistry
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.