2jw1

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Structural characterization of the type III pilotin-secretin interaction in Shigella flexneri by NMR spectroscopyStructural characterization of the type III pilotin-secretin interaction in Shigella flexneri by NMR spectroscopy

Structural highlights

2jw1 is a 2 chain structure with sequence from Shigella flexneri and Synthetic construct. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SCTG_SHIFL Involved in the synthesis of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (PubMed:10085046, PubMed:11717255). Pilot protein that is required for the proper localization of the secretin MxiD/SctC in the outer membrane (PubMed:11717255). Also influences both MxiD/SctC multimerization and stability (PubMed:11717255). Required for both Ipa translocation and tissue culture cell invasion (PubMed:10085046). Binds lipids (PubMed:15775974).[1] [2] [3]

Publication Abstract from PubMed

Assembly of the type-III secretion apparatus, which translocates proteins through both membranes of Gram-negative bacterial pathogens into host cells, requires the formation of an integral outer-membrane secretin ring. Typically, a small lipidated pilot protein is necessary for the stabilization and localization of this ring. Using NMR spectroscopy, we demonstrate that the C-terminal residues 553-570 of the Shigella flexneri secretin MxiD encompass the minimal binding domain for its cognate pilot MxiM. Although unstructured in isolation, upon complex formation with MxiM, these residues fold into an amphipathic turn-helix motif that caps the elongated hydrophobic cavity of the cracked beta-barrel pilot. Along with a rearrangement of core aromatic residues, this prevents the binding of lipids within the cavity. The mutually exclusive association of lipids and MxiD with MxiM establishes a framework for understanding the role of a pilot in the outer-membrane insertion and multimerization of the secretin ring.

Structural characterization of the type-III pilot-secretin complex from Shigella flexneri.,Okon M, Moraes TF, Lario PI, Creagh AL, Haynes CA, Strynadka NC, McIntosh LP Structure. 2008 Oct 8;16(10):1544-54. PMID:18940609[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Schuch R, Maurelli AT. The mxi-Spa type III secretory pathway of Shigella flexneri requires an outer membrane lipoprotein, MxiM, for invasin translocation. Infect Immun. 1999 Apr;67(4):1982-91. doi: 10.1128/IAI.67.4.1982-1991.1999. PMID:10085046 doi:http://dx.doi.org/10.1128/IAI.67.4.1982-1991.1999
  2. ↑ Schuch R, Maurelli AT. MxiM and MxiJ, base elements of the Mxi-Spa type III secretion system of Shigella, interact with and stabilize the MxiD secretin in the cell envelope. J Bacteriol. 2001 Dec;183(24):6991-8. doi: 10.1128/JB.183.24.6991-6998.2001. PMID:11717255 doi:http://dx.doi.org/10.1128/JB.183.24.6991-6998.2001
  3. ↑ Lario PI, Pfuetzner RA, Frey EA, Creagh L, Haynes C, Maurelli AT, Strynadka NC. Structure and biochemical analysis of a secretin pilot protein. EMBO J. 2005 Mar 23;24(6):1111-21. Epub 2005 Mar 10. PMID:15775974 doi:7600610
  4. ↑ Okon M, Moraes TF, Lario PI, Creagh AL, Haynes CA, Strynadka NC, McIntosh LP. Structural characterization of the type-III pilot-secretin complex from Shigella flexneri. Structure. 2008 Oct 8;16(10):1544-54. PMID:18940609 doi:http://dx.doi.org/S0969-2126(08)00333-X
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