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| | <StructureSection load='7jmu' size='340' side='right'caption='[[7jmu]], [[Resolution|resolution]] 1.20Å' scene=''> | | <StructureSection load='7jmu' size='340' side='right'caption='[[7jmu]], [[Resolution|resolution]] 1.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7jmu]] is a 2 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=7JMU OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7JMU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7jmu]] is a 2 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=7JMU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JMU FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2Å</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> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=7jmu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jmu OCA], [http://pdbe.org/7jmu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7jmu RCSB], [http://www.ebi.ac.uk/pdbsum/7jmu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7jmu 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=7jmu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jmu OCA], [https://pdbe.org/7jmu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7jmu RCSB], [https://www.ebi.ac.uk/pdbsum/7jmu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7jmu 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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 7jmu" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 7jmu" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Lysozyme 3D structures|Lysozyme 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | [[Category: Gallus gallus]] | | [[Category: Gallus gallus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lysozyme]]
| + | [[Category: Darmanin C]] |
| - | [[Category: Darmanin, C]] | + | [[Category: Drummond C]] |
| - | [[Category: Drummond, C]] | + | [[Category: Greaves T]] |
| - | [[Category: Greaves, T]] | + | [[Category: Han Q]] |
| - | [[Category: Han, Q]] | + | [[Category: Smith K]] |
| - | [[Category: Smith, K]] | + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Ionic liquid]]
| + | |
| - | [[Category: Nitrate]]
| + | |
| 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]
Publication Abstract from PubMed
Solvents that support protein functionality are important for biochemical applications, and new solvents are required. Here we employ FTIR and fluorescence spectroscopies, small angle X-ray scattering (SAXS) and X-ray crystallography to understand conformational changes of lysozyme with ionic liquids (ILs) added. Spectroscopic techniques identified that the secondary structure of lysozyme was maintained at the lower IL concentrations of 1 and 5 mol%, though the Tryptophan environment was significantly altered with nitrate-based ILs present. SAXS experiments indicated that the radius of gyration of lysozyme increased with 1 mol% IL present, and then decreased with increasing IL concentrations. The tertiary structure, particularly the loop regions, changed as a function of IL concentration, and this depended on the IL type. The crystallographic structure of lysozyme with the IL of ethylammonium nitrate present confirmed the loop region was extended, and identified three specific binding sites with nitrate ions, and that the positively charged areas were IL sensitive regions. This work provides a detailed understanding of lysozyme conformational changes in the presence of ILs. This approach can be extended to other functionally-important proteins.
Lysozyme conformational changes with ionic liquids: Spectroscopic, small angle x-ray scattering and crystallographic study.,Han Q, Smith KM, Darmanin C, Ryan TM, Drummond CJ, Greaves TL J Colloid Interface Sci. 2020 Oct 13. pii: S0021-9797(20)31347-3. doi:, 10.1016/j.jcis.2020.10.024. PMID:33109332[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
- ↑ Han Q, Smith KM, Darmanin C, Ryan TM, Drummond CJ, Greaves TL. Lysozyme conformational changes with ionic liquids: Spectroscopic, small angle x-ray scattering and crystallographic study. J Colloid Interface Sci. 2020 Oct 13. pii: S0021-9797(20)31347-3. doi:, 10.1016/j.jcis.2020.10.024. PMID:33109332 doi:http://dx.doi.org/10.1016/j.jcis.2020.10.024
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