1h6m

Covalent glycosyl-enzyme intermediate of hen egg white lysozymeCovalent glycosyl-enzyme intermediate of hen egg white lysozyme

Structural highlights 1h6m is a 1 chain structure with sequence from Chick. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: , , Related: 1w6z, 1kxx, 4lyo, 3lyo, 1kip, 1t6v, 1ic7, 1vds, 1lzt, 1kir, 2xbr, 1lys, 1bwj, 132l, 1e8l, 1yil, 1heo, 1sfg, 1kxw, 2x0a, 2c8o, 1yl1, 1sf4, 1g7l, 1ior, 1h87, 1ljg, 3lyt, 1dpx, 1iot, 1v7s, 1ja6, 1jis, 1ir8, 2w1m, 1uic, 1xgq, 1ykz, 1uie, 2war, 1lji, 8lyz, 1lj3, 1dpw, 2lyo, 2iff, 1bwi, 1g7h, 1jj0, 1lks, 1rfp, 5lyt, 1jiy, 1sfb, 1iee, 1xei, 1ir7, 1xek, 1hel, 1at6, 1ljf, 1mlc, 1f10, 2b5z, 193l, 1lsz, 1ljk, 6lyt, 1sq2, 1vdq, 1zmy, 2d91, 1lje, 2xth, 1b2k, 1lze, 1aki, 1hen, 1uia, 1yik, 1xfp, 2d6b, 1lpi, 1ndg, 1flw, 1lsd, 2blx, 6lyz, 1nbz, 1lsg, 4lyt, 1ved, 3hfm, 1jit, 1lzn, 1lyz, 1wtn, 1ja2, 1uuz, 2xbs, 2d4i, 2fbb, 2lym, 1fdl, 1gxx, 1lz9, 1lse, 1lzh, 1lsm, 3lym, 7lyz, 1jj3, 1yky, 1t3p, 1heq, 1kiq, 2lzh, 1uih, 1kxy, 2w1l, 2bly, 1b0d, 1g7j, 1bhz, 1her, 1wtm, 1hep, 1ioq, 1nby, 1jtt, 1qio, 1lza, 1xgp, 1ps5, 1gwd, 1v7t, 1jpo, 1dqj, 2a7d, 1j1p, 2c8p, 1z55, 1ljj, 1lsb, 1f0w, 2w1x, 1lzg, 1flq, 1lzc, 1jj1, 1rcm, 1uid, 1yqv, 1hsx, 1bgi, 1lcn, 1lzd, 1hew, 2cds, 2vb1, 2aub, 1hf4, 1uib, 1ir9, 2cgi, 1j1x, 1rjc, 1ios, 1uc0, 1azf, 1ljh, 1ic4, 4lyz, 1gpq, 2a6u, 2d4k, 1xej, 1ja7, 1mel, 1ri8, 1uig, 1bvx, 1qtk, 1c10, 1lkr, 1lyo, 2xjw, 1hsw, 1n4f, 2w1y, 1jto, 1g7m, 1sf7, 1lsf, 1fn5, 5lyz, 2d4j, 1c08, 3lzt, 1ndm, 1sf6, 3lyz, 1bvk, 1uif, 2lyz, 1vau, 1fly, 1lma, 1yl0, 1j1o, 1hc0, 2lzt, 4lzt, 1a2y, 1uco, 1lsy, 1lsa, 1ic5, 1p2c, 5lym, 1gxv, 1ua6, 1at5, 1f3j, 1vat, 1lj4, 1hem, 1vfb, 1ja4, 4lym, 2a7f, 194l, 1flu, 1lz8, 1ykx, 1bwh, 2hfm, 1vdt, 1io5, 1lsn, 1lzb, 2bpu, 1g7i, 1lsc, 1vdp Activity: Lysozyme, with EC number 3.2.1.17 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [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 Hen egg-white lysozyme (HEWL) was the first enzyme to have its three-dimensional structure determined by X-ray diffraction techniques. A catalytic mechanism, featuring a long-lived oxocarbenium-ion intermediate, was proposed on the basis of model-building studies. The 'Phillips' mechanism is widely held as the paradigm for the catalytic mechanism of beta-glycosidases that cleave glycosidic linkages with net retention of configuration of the anomeric centre. Studies with other retaining beta-glycosidases, however, provide strong evidence pointing to a common mechanism for these enzymes that involves a covalent glycosyl-enzyme intermediate, as previously postulated. Here we show, in three different cases using electrospray ionization mass spectrometry, a catalytically competent covalent glycosyl-enzyme intermediate during the catalytic cycle of HEWL. We also show the three-dimensional structure of this intermediate as determined by X-ray diffraction. We formulate a general catalytic mechanism for all retaining beta-glycosidases that includes substrate distortion, formation of a covalent intermediate, and the electrophilic migration of C1 along the reaction coordinate. Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate.,Vocadlo DJ, Davies GJ, Laine R, Withers SG Nature. 2001 Aug 23;412(6849):835-8. PMID:11518970 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Lysozyme 3D structures

spinqualitylabelsall models 1h6m, resolution 1.64Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image