2xbs

Raman crystallography of Hen White Egg Lysozyme - High X-ray dose (16 MGy)Raman crystallography of Hen White Egg Lysozyme - High X-ray dose (16 MGy)

Structural highlights 2xbs is a 1 chain structure with sequence from Gallus gallus. 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, 1lys, 132l, 1e8l, 1bwj, 1yil, 1heo, 1sfg, 1kxw, 2x0a, 2c8o, 1yl1, 1sf4, 1g7l, 1ior, 1h87, 3lyt, 1ljg, 1dpx, 1iot, 1v7s, 1ja6, 1jis, 1ir8, 2w1m, 1uic, 1xgq, 1ykz, 1uie, 2war, 1lji, 1lj3, 1dpw, 8lyz, 2lyo, 1bwi, 2iff, 1g7h, 1lks, 1jj0, 1rfp, 5lyt, 1sfb, 1jiy, 1ir7, 1iee, 1xei, 1xek, 1hel, 1at6, 1ljf, 1mlc, 2b5z, 1f10, 193l, 1lsz, 1ljk, 6lyt, 1sq2, 1vdq, 1zmy, 1lje, 2d91, 1lze, 1b2k, 1aki, 1hen, 1uia, 1xfp, 1yik, 2d6b, 1lpi, 1ndg, 1flw, 1lsd, 2blx, 6lyz, 1nbz, 1lsg, 4lyt, 3hfm, 1ved, 1jit, 1lzn, 1ja2, 1wtn, 1lyz, 1uuz, 2d4i, 2fbb, 2lym, 1fdl, 1gxx, 1lz9, 1lzh, 1lse, 1lsm, 1jj3, 7lyz, 3lym, 1yky, 1t3p, 1heq, 1kiq, 1kxy, 2lzh, 1uih, 2w1l, 2bly, 1b0d, 1g7j, 1her, 1bhz, 1wtm, 1hep, 1ioq, 1nby, 1jtt, 1qio, 1lza, 1ps5, 1xgp, 1gwd, 1jpo, 1v7t, 1h6m, 1dqj, 1j1p, 2a7d, 1z55, 2c8p, 1ljj, 1lsb, 1f0w, 2w1x, 1lzg, 1flq, 1lzc, 1jj1, 1rcm, 1yqv, 1uid, 1hsx, 1bgi, 1lzd, 1lcn, 1hew, 2vb1, 2cds, 2aub, 1uib, 1hf4, 2cgi, 1j1x, 1rjc, 1ios, 1ir9, 1uc0, 1azf, 1ljh, 1ic4, 4lyz, 1gpq, 2a6u, 2d4k, 1xej, 1ja7, 1mel, 1ri8, 1uig, 1bvx, 1qtk, 1c10, 1lkr, 1lyo, 1n4f, 1hsw, 1g7m, 1jto, 2w1y, 1sf7, 1lsf, 1fn5, 5lyz, 2d4j, 3lzt, 1c08, 1ndm, 1sf6, 3lyz, 1bvk, 1uif, 1vau, 2lyz, 1lma, 1fly, 1hc0, 1j1o, 1yl0, 2lzt, 1a2y, 4lzt, 1uco, 1lsy, 1lsa, 1p2c, 1gxv, 5lym, 1ic5, 1ua6, 1at5, 1vat, 1hem, 1vfb, 1f3j, 1lj4, 1ja4, 2a7f, 4lym, 194l, 1flu, 1lz8, 1ykx, 1vdt, 1bwh, 2hfm, 1io5, 1lsn, 1lzb, 1g7i, 2bpu, 1lsc, 1vdp, 2xbr 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. Publication Abstract from PubMed X-ray-induced chemistry modifies biological macromolecules structurally and functionally, even at cryotemperatures. The mechanisms of x-radiation damage in colored or redox proteins have often been investigated by combining X-ray crystallography with in crystallo ultraviolet-visible spectroscopy. Here, we used Raman microspectrophotometry to follow the onset of damage in crystalline lysozyme, notably that of disulfide bond breakage. The dose-dependent Raman spectra are consistent with a kinetic model for the rupture of disulfide bonds suggesting the rapid build up of an anionic radical intermediate. This intermediate may either revert back to the oxidized state or evolve toward protonated radical species or cleaved products. The data strongly suggest that back conversion of the anionic radical is significantly accelerated by X-rays, revealing an X-ray-induced "repair" mechanism. The possibility of X-ray-induced chemical repair is an important feature to take into account when assessing radiation damage in macromolecules. Raman-assisted crystallography suggests a mechanism of x-ray-induced disulfide radical formation and reparation.,Carpentier P, Royant A, Weik M, Bourgeois D Structure. 2010 Nov 10;18(11):1410-9. PMID:21070940 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Lysozyme 3D structures

spinqualitylabelsall models 2xbs, resolution 1.37Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image