3VJP

Orthorhombic Crystal Structure of Salmonella FlgA in closed form

Summary for 3VJP

• Entry DOI: 10.2210/pdb3vjp/pdb
• Related: 3TEE
• Descriptor: Flagella basal body P-ring formation protein flgA (2 entities in total)
• Functional Keywords: bacterial flagellum, secretion, disulfide bond, chaperone
• Biological source: Salmonella typhimurium
• Cellular location: Periplasm : P40131
• Total number of polymer chains: 2
• Total formula weight: 47686.60

Authors

Matsunami, H.,Samatey, F.A.,Namba, K. (deposition date: 2011-10-27, release date: 2012-10-31, Last modification date: 2016-07-06)

Primary citation

Matsunami, H.,Yoon, Y.H.,Meshcheryakov, V.A.,Namba, K.,Samatey, F.A.
Structural flexibility of the periplasmic protein, FlgA, regulates flagellar P-ring assembly in Salmonella enterica
Sci Rep, 6:27399-27399, 2016

PubMed Abstract: A periplasmic flagellar chaperone protein, FlgA, is required for P-ring assembly in bacterial flagella of taxa such as Salmonella enterica or Escherichia coli. The mechanism of chaperone-mediated P-ring formation is poorly understood. Here we present the open and closed crystal structures of FlgA from Salmonella enterica serovar Typhimurium, grown under different crystallization conditions. An intramolecular disulfide cross-linked form of FlgA caused a dominant negative effect on motility of the wild-type strain. Pull-down experiments support a specific protein-protein interaction between FlgI, the P-ring component protein, and the C-terminal domain of FlgA. Surface plasmon resonance and limited-proteolysis indicate that flexibility of the domain is reduced in the covalently closed form. These results show that the structural flexibility of the C-terminal domain of FlgA, which is related to the structural difference between the two crystal forms, is intrinsically associated with its molecular chaperone function in P-ring assembly.

PubMed: 27273476
DOI: 10.1038/srep27399

Experimental method

X-RAY DIFFRACTION (2.7 Å)