5B3D
Structure of a flagellar type III secretion chaperone, FlgN
Summary for 5B3D
Entry DOI | 10.2210/pdb5b3d/pdb |
Descriptor | Flagella synthesis protein FlgN (2 entities in total) |
Functional Keywords | flagellar type iii secretion, export chaperone, four-stranded coiled coil, protein transport |
Biological source | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
Total number of polymer chains | 4 |
Total formula weight | 64593.83 |
Authors | Nakanishi, Y.,Kinoshita, M.,Namba, K.,Minamino, T.,Imada, K. (deposition date: 2016-02-15, release date: 2016-06-01, Last modification date: 2020-02-26) |
Primary citation | Kinoshita, M.,Nakanishi, Y.,Furukawa, Y.,Namba, K.,Imada, K.,Minamino, T. Rearrangements of alpha-helical structures of FlgN chaperone control the binding affinity for its cognate substrates during flagellar type III export Mol.Microbiol., 101:656-670, 2016 Cited by PubMed: 27178222DOI: 10.1111/mmi.13415 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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