2jw1

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

spinqualitylabelsall models 2jw1 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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, 15 models Ligands: ACE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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