Crystal structures of two camelid nanobodies raised against GldL, a component of the type IX secretion system from Flavobacterium johnsoniae
| Autor: | Philippe Leone, Anaïs Gaubert, Alain Roussel, Pauline Melani, Christian Cambillau, Thi Trang Nhung Trinh |
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| Rok vydání: | 2021 |
| Předmět: |
Models
Molecular Camelus Gliding motility Biophysics Context (language use) Crystal structure Crystallography X-Ray Biochemistry Flavobacterium Research Communications 03 medical and health sciences Bacterial Proteins Protein Domains Structural Biology Genetics Animals Scattering Radiation Molecular replacement Secretion Flavobacterium johnsoniae Bacterial Secretion Systems 030304 developmental biology 0303 health sciences 030306 microbiology Chemistry Single-Domain Antibodies Condensed Matter Physics Kinetics Cytoplasm Thermodynamics Protein Multimerization Function (biology) |
| Zdroj: | Acta Crystallogr F Struct Biol Commun |
| ISSN: | 2053-230X |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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