1uuz | pdb_00001uuz

IVY:A NEW FAMILY OF PROTEIN

spinqualitylabelsall models 1uuz, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1uuz is a 4 chain structure with sequence from "bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885 and Gallus gallus. This structure supersedes the now removed PDB entry 1hke. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 132l, 193l, 194l, 1a2y, 1aki, 1at5, 1at6, 1azf, 1b0d, 1b2k, 1bgi, 1bhz, 1bvk, 1bvx, 1bwh, 1bwi, 1bwj, 1c08, 1c10, 1dpw, 1dpx, 1dqj, 1e8l, 1f0w, 1f10, 1f3j, 1fdl, 1flq, 1flu, 1flw, 1fly, 1fn5, 1g7h, 1g7i, 1g7j, 1g7l, 1g7m, 1gpq, 1gwd, 1gxv, 1gxx, 1h6m, 1h87, 1hc0, 1hel, 1hem, 1hen, 1heo, 1hep, 1heq, 1her, 1hew, 1hf4, 1hsw, 1hsx, 1ic4, 1ic5, 1ic7, 1iee, 1io5, 1ioq, 1ior, 1ios, 1iot, 1ir7, 1ir8, 1ir9, 1j1o, 1j1p, 1j1x, 1ja2, 1ja4, 1ja6, 1ja7, 1jis, 1jit, 1jiy, 1jj0, 1jj1, 1jj3, 1jpo, 1jto, 1jtt, 1kip, 1kiq, 1kir, 1kxw, 1kxx, 1kxy, 1lcn, 1lj3, 1lj4, 1lje, 1ljf, 1ljg, 1ljh, 1lji, 1ljj, 1ljk, 1lkr, 1lks, 1lma, 1lpi, 1lsa, 1lsb, 1lsc, 1lsd, 1lse, 1lsf, 1lsg, 1lsm, 1lsn, 1lsy, 1lsz, 1lyo, 1lys, 1lyz, 1lz8, 1lz9, 1lza, 1lzb, 1lzc, 1lzd, 1lze, 1lzg, 1lzh, 1lzn, 1lzt, 1mel, 1mlc, 1n4f, 1nby, 1nbz, 1ndg, 1ndm, 1ps5, 1qio, 1qtk, 1rcm, 1rfp, 1uc0, 1uco, 1uia, 1uib, 1uic, 1uid, 1uie, 1uif, 1uig, 1uih, 1vfb, 1xei, 1xej, 1xek, 2cds, 2hfm, 2iff, 2lym, 2lyo, 2lyz, 2lzh, 2lzt, 3hfl, 3hfm, 3lym, 3lyo, 3lyt, 3lyz, 3lzt, 4lym, 4lyo, 4lyt, 4lyz, 4lzt, 5lym, 5lyt, 5lyz, 6lyt, 6lyz, 7lyz, 8lyz Activity: Lysozyme, with EC number 3.2.1.17 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [IVY_PSEAE] Strong inhibitor of lysozyme C. [LYSC_CHICK] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Part of an ancestral bactericidal system, vertebrate C-type lysozyme targets the peptidoglycan moiety of bacterial cell walls. We report the crystal structure of a protein inhibitor of C-type lysozyme, the Escherichia coli Ivy protein, alone and in complex with hen egg white lysozyme. Ivy exhibits a novel fold in which a protruding five-residue loop appears essential to its inhibitory effect. This feature guided the identification of Ivy orthologues in other Gram-negative bacteria. The structure of the evolutionary distant Pseudomonas aeruginosa Ivy orthologue was also determined in complex with hen egg white lysozyme, and its antilysozyme activity was confirmed. Ivy expression protects porous cell-wall E. coli mutants from the lytic effect of lysozyme, suggesting that it is a response against the permeabilizing effects of the innate vertebrate immune system. As such, Ivy acts as a virulence factor for a number of Gram-negative bacteria-infecting vertebrates. Structure and evolution of the Ivy protein family, unexpected lysozyme inhibitors in Gram-negative bacteria.,Abergel C, Monchois V, Byrne D, Chenivesse S, Lembo F, Lazzaroni JC, Claverie JM Proc Natl Acad Sci U S A. 2007 Apr 10;104(15):6394-9. Epub 2007 Apr 3. PMID:17405861 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Lysozyme 3D structures

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