Structural highlights
Function
[SPAK_SHIFL] Required for surface presentation of invasion plasmid antigens. Chaperone specialized in the storage of effectors within the bacterial cytoplasm, maintaining them in a secretion-competent state, and allowing their immediate delivery to target cells upon contact of the bacterium with the host cells. Has been shown to chaperone IpaA, IpgB1, OspC3 and probably also OspB.
Publication Abstract from PubMed
Shigella flexneri Spa15 is a chaperone of the type 3 secretion system, which binds a number of effectors to ensure their stabilization prior to secretion. One of these effectors is IpgB1, a mimic of the human Ras-like Rho guanosine triphosphatase RhoG. In this study, Spa15 alone and in complex with IpgB1 has been studied by double electron electron resonance, an experiment that gives distance information showing the spacial separation of attached spin labels. This distance is explained by determining the crystal structure of the spin-labeled Spa15 where labels are seen to be buried in hydrophobic pockets. The double electron electron resonance experiment on the Spa15 complex with IpgB1 shows that IpgB1 does not bind Spa15 in the same way as is seen in the homologous Salmonella sp. chaperone:effector complex InvB:SipA.
Shigella flexneri Spa15 Crystal Structure Verified in Solution by Double Electron Electron Resonance.,Lillington JE, Lovett JE, Johnson S, Roversi P, Timmel CR, Lea SM J Mol Biol. 2010 Nov 12. PMID:21075116[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lillington JE, Lovett JE, Johnson S, Roversi P, Timmel CR, Lea SM. Shigella flexneri Spa15 Crystal Structure Verified in Solution by Double Electron Electron Resonance. J Mol Biol. 2010 Nov 12. PMID:21075116 doi:10.1016/j.jmb.2010.10.053
