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| | ==pH evolution of tetragonal HEWL at 4 degrees Celcius.== | | ==pH evolution of tetragonal HEWL at 4 degrees Celcius.== |
| - | <StructureSection load='2a6u' size='340' side='right' caption='[[2a6u]]' scene=''> | + | <StructureSection load='2a6u' size='340' side='right'caption='[[2a6u]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2a6u]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A6U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2A6U FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2a6u]] 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=2A6U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A6U FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray powder diffraction</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2a6u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a6u OCA], [http://pdbe.org/2a6u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2a6u RCSB], [http://www.ebi.ac.uk/pdbsum/2a6u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2a6u ProSAT]</span></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=2a6u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a6u OCA], [https://pdbe.org/2a6u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a6u RCSB], [https://www.ebi.ac.uk/pdbsum/2a6u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a6u ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> | + | [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/a6/2a6u_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a6/2a6u_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <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> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Gallus gallus]] | | [[Category: Gallus gallus]] |
| - | [[Category: Lysozyme]] | + | [[Category: Large Structures]] |
| - | [[Category: Margiolaki, I]] | + | [[Category: Margiolaki I]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Powder diffraction]]
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| - | [[Category: Rietveld refinement]]
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| Structural highlights
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
44 samples of tetragonal hen egg-white lysozyme (HEWL) were obtained as a series of polycrystalline precipitates at 277 K and room temperature in the pH range between 6.56 and 3.33. The precipitates were investigated by the collection of high-resolution powder X-ray diffraction data at 295 K, which reveal the tetragonal or orthorhombic forms of lysozyme depending on the temperature and pH of crystallization. The use of a new robotic sample changer greatly facilitated these measurements. LeBail analyses of the powder patterns display a characteristic behaviour for the pH dependence of the tetragonal unit-cell parameters of HEWL crystallized at both temperatures. More detailed analysis shows that molecular replacement can give a suitable starting point for structural refinements, illustrating that powder data can be sufficient for this approach. Pawley or Rietveld refinements that fit a single model to four data sets simultaneously from four samples crystallized at pH values across the range studied benefit from improved powder data quality via the anisotropic changes in the unit cell. The Rietveld analysis gave an average structural model with excellent goodness of fit and stereochemistry.
High-throughput phase-diagram mapping via powder diffraction: a case study of HEWL versus pH.,Basso S, Fitch AN, Fox GC, Margiolaki I, Wright JP Acta Crystallogr D Biol Crystallogr. 2005 Dec;61(Pt 12):1612-25. Epub 2005, Nov 19. PMID:16301795[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
- ↑ Basso S, Fitch AN, Fox GC, Margiolaki I, Wright JP. High-throughput phase-diagram mapping via powder diffraction: a case study of HEWL versus pH. Acta Crystallogr D Biol Crystallogr. 2005 Dec;61(Pt 12):1612-25. Epub 2005, Nov 19. PMID:16301795 doi:10.1107/S0907444905031963
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