3VJP: Orthorhombic Crystal Structure Of Salmonella Flga In Closed Form

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.
PDB ID: 3VJPDownload
MMDB ID: 104467
PDB Deposition Date: 2011/10/27
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 2.7  Å
Source Organism:
Similar Structures:
Biological Unit for 3VJP: monomeric; determined by author and by software (PISA)
Molecular Components in 3VJP
Label Count Molecule
Protein (1 molecule)
Flagella Basal Body P-ring Formation Protein Flga(Gene symbol: flgA)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB