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: 27178222 DOI: 10.1111/mmi.13415 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.3 Å)

Structure validation