2c8o: Difference between revisions
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<StructureSection load='2c8o' size='340' side='right'caption='[[2c8o]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='2c8o' size='340' side='right'caption='[[2c8o]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2c8o]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2c8o]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C8O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C8O FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2c8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c8o OCA], [https://pdbe.org/2c8o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c8o RCSB], [https://www.ebi.ac.uk/pdbsum/2c8o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c8o ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/LYSC_CHICK 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.<ref>PMID:22044478</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c8/2c8o_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c8/2c8o_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| Line 38: | Line 37: | ||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Bourgeois D]] | |||
[[Category: Bourgeois | [[Category: Cipriani F]] | ||
[[Category: Cipriani | [[Category: Felisaz F]] | ||
[[Category: Felisaz | [[Category: Jacquamet L]] | ||
[[Category: Jacquamet | [[Category: Joly J]] | ||
[[Category: Joly | [[Category: Lavault B]] | ||
[[Category: Lavault | [[Category: Nurizzo D]] | ||
[[Category: Nurizzo | [[Category: Ohana J]] | ||
[[Category: Ohana | [[Category: Vernede X]] | ||
[[Category: Vernede | |||
Latest revision as of 10:48, 23 October 2024
lysozyme (1sec) and UV lasr excited fluorescencelysozyme (1sec) and UV lasr excited fluorescence
Structural highlights
FunctionLYSC_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 PubMedStructural 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 AlsoReferences
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