3da4

Crystal Structure of Colicin M, a Novel Phosphatase Specifically Imported by Escherichia Coli

spinqualitylabelsall models 3da4, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3da4 is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7Å Ligands: NO3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CEAM_ECOLX Colicins are polypeptide toxins produced by and active against E.coli and closely related bacteria. This is a calcium-requiring inhibitor for murein biosynthesis; it causes lysis of sensitive cells accompanied by murein degradation. The target site is possibly the cytoplasmic membrane. Publication Abstract from PubMed Colicins are cytotoxic proteins secreted by certain strains of Escherichia coli. Colicin M is unique among these toxins in that it acts in the periplasm and specifically inhibits murein biosynthesis by hydrolyzing the pyrophosphate linkage between bactoprenol and the murein precursor. We crystallized colicin M and determined the structure at 1.7 A resolution using X-ray crystallography. The protein has a novel structure composed of three domains with distinct functions. The N-domain is a short random coil and contains the exposed TonB box. The central domain includes a hydrophobic -helix and binds presumably to the FhuA receptor. The C-domain is composed of a mixed -domain and forms the phosphatase. The architectures of the individual modules show no similarity to known structures. Amino acid replacements in previously isolated inactive colicin M mutants are located in the phosphatase domain, which contains a number of surface-exposed residues conserved in predicted bacteriocins of other bacteria. The novel phosphatase domain displays no sequence similarity to known phosphatases. The N-terminal and central domains are not conserved among bacteriocins, which likely reflect the distinct import proteins required for the uptake of the various bacteriocins. The homology pattern supports our previous proposal that colicins evolved by combination of distinct functional domains. Crystal structure of colicin M, a novel phosphatase specifically imported by Escherichia coli.,Zeth K, Romer C, Patzer SI, Braun V J Biol Chem. 2008 Jul 18. PMID:18640984 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Colicin 3D structures

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