4gdn | pdb_00004gdn

Structure of FmtA-like protein

spinqualitylabelsall models 4gdn, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4gdn is a 4 chain structure with sequence from Staan. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PE4 Related: 3o3v Gene: flp, SA2230 (STAAN) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [FLP_STAAN] Its precise function is unknown. Has no penicillin-binding activity and is not involved in methicillin resistance (By similarity). Publication Abstract from PubMed pks genomic island of Escherichia coli is involved in the synthesis of the non-ribosomal peptide-type genotoxin colibactin, which has been suggesting as affecting the host immune response and having an impact on cancer development. The pks-encoded enzyme ClbP is an atypical peptidase that contributes to the synthesis of colibactin. In this work, we identified key features of ClbP. Bacterial fractionation and Western-blot analysis revealed the docking of ClbP to the bacterial inner membrane via a C-terminal domain harboring three predicted transmembrane helices. Whereas only one helix was necessary for the location in the inner membrane, the complete sequence of the C-terminal domain was necessary for ClbP bioactivity. In addition, the N-terminal sequence of ClbP allowed the SRP/Sec/YidC- and MreB-dependent translocation of the enzymatic domain in the periplasmic compartment, a feature also essential for ClbP bioactivity. Finally, the comparison of ClbP structure with that of the paralogs FmtA-like and AmpC revealed at an extremity of the catalytic groove a negative electrostatic potential surface characteristic of ClbP. Site-directed mutagenesis experiments identified in this zone two aspartic residues that were important for ClbP bioactivity. Overall, these results suggest a model for precolibactin activation by ClbP and pave a way for the design of inhibitors targeting colibactin production. Analysis of Structure-Function Relationships in the Colibactin-Maturating Enzyme ClbP.,Cougnoux A, Gibold L, Robin F, Dubois D, Pradel N, Darfeuille-Michaud A, Dalmasso G, Delmas J, Bonnet R J Mol Biol. 2012 Oct 2. pii: S0022-2836(12)00782-6. doi:, 10.1016/j.jmb.2012.09.017. PMID:23041299 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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