2b5z
From Proteopedia
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| - | [[Image:2b5z.jpg|left|200px]] | ||
| - | < | + | ==Hen lysozyme chemically glycosylated== |
| - | + | <StructureSection load='2b5z' size='340' side='right'caption='[[2b5z]], [[Resolution|resolution]] 1.60Å' scene=''> | |
| - | You may | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[2b5z]] 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=2B5Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B5Z FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> | |
| - | -- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AZI:AZIDE+ION'>AZI</scene>, <scene name='pdbligand=BGS:BETA-D-GLUCOPYRANOSYLSULFONYLETHANE'>BGS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=2b5z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b5z OCA], [https://pdbe.org/2b5z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b5z RCSB], [https://www.ebi.ac.uk/pdbsum/2b5z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b5z ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == 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 == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b5/2b5z_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2b5z ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The crystallization of glycoproteins is one of the challenges to be confronted by the crystallographic community in the frame of what is known as glycobiology. The state of the art for the crystallization of glycoproteins is not promising and removal of the carbohydrate chains is generally suggested since they are flexible and a source of heterogeneity. In this paper, the feasibility of introducing glucose into the model protein hen egg-white lysozyme via a post-purification glycosylation reaction that may turn any protein into a model glycoprotein whose carbohydrate fraction can be manipulated is demonstrated. | ||
| - | + | Production, crystallization and X-ray characterization of chemically glycosylated hen egg-white lysozyme.,Lopez-Jaramillo FJ, Perez-Banderas F, Hernandez-Mateo F, Santoyo-Gonzalez F Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Apr 1;61(Pt 4):435-8. doi: , 10.1107/S1744309105008869. Epub 2005 Apr 1. PMID:16511062<ref>PMID:16511062</ref> | |
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2b5z" style="background-color:#fffaf0;"></div> | ||
| - | == | + | ==See Also== |
| - | + | *[[Lysozyme 3D structures|Lysozyme 3D structures]] | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | + | [[Category: Hernandez-Mateo F]] | |
| - | [[Category: Hernandez-Mateo | + | [[Category: Lopez-Jaramillo FJ]] |
| - | [[Category: Lopez-Jaramillo | + | [[Category: Perez-Balderas F]] |
| - | [[Category: Perez-Balderas | + | [[Category: Santoyo-Gonzalez F]] |
| - | [[Category: Santoyo-Gonzalez | + | |
| - | + | ||
| - | + | ||
Current revision
Hen lysozyme chemically glycosylated
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