| Structural highlights
2c8o 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.
| | 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, 1p2c, 1ps5, 1qio, 1qtk, 1rcm, 1rfp, 1ri8, 1rjc, 1sf4, 1sf6, 1sf7, 1sfb, 1sfg, 1sq2, 1t3p, 1t6v, 1ua6, 1uc0, 1uco, 1uia, 1uib, 1uic, 1uid, 1uie, 1uif, 1uig, 1uih, 1uuz, 1v7s, 1v7t, 1vat, 1vau, 1vdp, 1vdq, 1vds, 1vdt, 1ved, 1vfb, 1w6z, 1wtm, 1wtn, 1xei, 1xej, 1xek, 1xfp, 1xgp, 1xgq, 1yik, 1yil, 1ykx, 1yky, 1ykz, 1yl0, 1yl1, 1yqv, 1z55, 1zmy, 2a7d, 2a7f, 2blx, 2bly, 2bpu, 2cds, 2d6b, 2hfm, 2iff, 2lym, 2lyo, 2lyz, 2lzh, 2lzt, 3hfm, 3lym, 3lyo, 3lyt, 3lyz, 3lzt, 4lym, 4lyo, 4lyt, 4lyz, 4lzt, 5lym, 5lyt, 5lyz, 6lyt, 6lyz, 7lyz, 8lyz, 2c8p |
| 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]
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
Structural proteomics has promoted the rapid development of automated protein structure determination using X-ray crystallography. Robotics are now routinely used along the pipeline from genes to protein structures. However, a bottleneck still remains. At synchrotron beamlines, the success rate of automated sample alignment along the X-ray beam is limited by difficulties in visualization of protein crystals, especially when they are small and embedded in mother liquor. Despite considerable improvement in optical microscopes, the use of visible light transmitted or reflected by the sample may result in poor or misleading contrast. Here, the endogenous fluorescence from aromatic amino acids has been used to identify even tiny or weakly fluorescent crystals with a high success rate. The use of a compact laser at 266 nm in combination with non-fluorescent sample holders provides an efficient solution to collect high-contrast fluorescence images in a few milliseconds and using standard camera optics. The best image quality was obtained with direct illumination through a viewing system coaxial with the UV beam. Crystallographic data suggest that the employed UV exposures do not generate detectable structural damage.
UV laser-excited fluorescence as a tool for the visualization of protein crystals mounted in loops.,Vernede X, Lavault B, Ohana J, Nurizzo D, Joly J, Jacquamet L, Felisaz F, Cipriani F, Bourgeois D Acta Crystallogr D Biol Crystallogr. 2006 Mar;62(Pt 3):253-61. Epub 2006, Feb 22. PMID:16510972[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
- ↑ Vernede X, Lavault B, Ohana J, Nurizzo D, Joly J, Jacquamet L, Felisaz F, Cipriani F, Bourgeois D. UV laser-excited fluorescence as a tool for the visualization of protein crystals mounted in loops. Acta Crystallogr D Biol Crystallogr. 2006 Mar;62(Pt 3):253-61. Epub 2006, Feb 22. PMID:16510972 doi:http://dx.doi.org/10.1107/S0907444905041429
|
