| Structural highlights
2xbs 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, 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.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Maehashi K, Matano M, Irisawa T, Uchino M, Kashiwagi Y, Watanabe T. Molecular characterization of goose- and chicken-type lysozymes in emu (Dromaius novaehollandiae): evidence for extremely low lysozyme levels in emu egg white. Gene. 2012 Jan 15;492(1):244-9. doi: 10.1016/j.gene.2011.10.021. Epub 2011 Oct, 25. PMID:22044478 doi:10.1016/j.gene.2011.10.021
- ↑ Carpentier P, Royant A, Weik M, Bourgeois D. Raman-assisted crystallography suggests a mechanism of x-ray-induced disulfide radical formation and reparation. Structure. 2010 Nov 10;18(11):1410-9. PMID:21070940 doi:10.1016/j.str.2010.09.010
|
