2fm8

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Crystal Structure of the Salmonella Secretion Chaperone InvB in Complex with SipA

Structural highlights

2fm8 is a 3 chain structure with sequence from Salmonella enterica subsp. enterica serovar Typhimurium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SPAK_SALTY Involved in a secretory pathway responsible for the surface presentation of determinants needed for the entry of Salmonella species into mammalian cells. 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 SopA, SopE, SopE2 and SipA.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Higashide W, Zhou D. The first 45 amino acids of SopA are necessary for InvB binding and SPI-1 secretion. J Bacteriol. 2006 Apr;188(7):2411-20. PMID:16547027 doi:http://dx.doi.org/10.1128/JB.188.7.2411-2420.2006
  2. ↑ Lilic M, Vujanac M, Stebbins CE. A common structural motif in the binding of virulence factors to bacterial secretion chaperones. Mol Cell. 2006 Mar 3;21(5):653-64. PMID:16507363 doi:10.1016/j.molcel.2006.01.026

Contents


PDB ID 2fm8

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