4k0u | pdb_00004k0u

Pilotin/secretin peptide Complex

spinqualitylabelsall models 4k0u, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4k0u is a 2 chain structure with sequence from Dicd3. This structure supersedes the now removed PDB entry 3uym. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 3utk Gene: Dda3937_02411, outS, OutS Dda3937_02411 (DICD3) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [OUTS_DICD3] Out proteins are required for the translocation of pectate lyases and cellulases across the outer membrane. [GSPD2_DICD3] Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of proteins (By similarity). Required for the translocation of the multiple pectic enzymes. Publication Abstract from PubMed The secretins are a family of large multimeric channels in the outer membrane of Gram-negative bacteria that are involved in protein export. In Dickeya dadantii and many other pathogenic bacteria, the lipoprotein pilotin targets the secretin subunits to the outer membrane, allowing a functional type II secretion system to be assembled. Here, the crystal structure of the C-terminal peptide of the secretin subunit bound to its cognate pilotin is reported. In solution, this C-terminal region of the secretin is nonstructured. The secretin peptide folds on binding to the pilotin to form just under four turns of alpha-helix which bind tightly up against the first helix of the pilotin so that the hydrophobic residues of the secretin helix can bind to the hydrophobic surface of the pilotin. The secretin helix binds parallel to the first part of the fourth helix of the pilotin. An N-capping aspartate encourages helix formation and binding by interacting favourably with the helix dipole of the helical secretin peptide. The structure of the secretin-pilotin complex of the phytopathogenic D. dadantii described here is a paradigm for this interaction in the OutS-PulS family of pilotins, which is essential for the correct assembly of the type II secretion system of several potent human adversaries, including enterohaemorrhagic Escherichia coli and Klebsiella oxytoca. Anatomy of secretin binding to the Dickeya dadantii type II secretion system pilotin.,Rehman S, Gu S, Shevchik VE, Pickersgill RW Acta Crystallogr D Biol Crystallogr. 2013 Aug;69(Pt 8):1381-6. doi:, 10.1107/S0907444913007658. Epub 2013 Jul 13. PMID:23897461 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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