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| | <StructureSection load='1xgu' size='340' side='right'caption='[[1xgu]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='1xgu' size='340' side='right'caption='[[1xgu]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1xgu]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Chick Chick] and [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XGU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XGU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1xgu]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XGU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XGU FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1xgp|1xgp]], [[1xgq|1xgq]], [[1xgr|1xgr]], [[1xgt|1xgt]]</div></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]] 2.1Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </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=1xgu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xgu OCA], [https://pdbe.org/1xgu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xgu RCSB], [https://www.ebi.ac.uk/pdbsum/1xgu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xgu 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=1xgu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xgu OCA], [https://pdbe.org/1xgu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xgu RCSB], [https://www.ebi.ac.uk/pdbsum/1xgu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xgu ProSAT]</span></td></tr> |
| | </table> | | </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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chick]] | + | [[Category: Gallus gallus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Lysozyme]]
| + | [[Category: Huang Y]] |
| - | [[Category: Huang, Y]] | + | [[Category: Li Y]] |
| - | [[Category: Li, Y]] | + | [[Category: Mariuzza RA]] |
| - | [[Category: Mariuzza, R A]] | + | [[Category: Smith-Gill SJ]] |
| - | [[Category: Smith-Gill, S J]] | + | [[Category: Swaminathan CP]] |
| - | [[Category: Swaminathan, C P]] | + | |
| - | [[Category: 1a crystal structure]]
| + | |
| - | [[Category: Hyhel-63]]
| + | |
| - | [[Category: Immune system]]
| + | |
| - | [[Category: Y33f mutant]]
| + | |
| 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
Hydrophobic interactions are essential for stabilizing protein-protein complexes, whose interfaces generally consist of a central cluster of hot spot residues surrounded by less important peripheral residues. According to the O-ring hypothesis, a condition for high affinity binding is solvent exclusion from interacting residues. This hypothesis predicts that the hydrophobicity at the center is significantly greater than at the periphery, which we estimated at 21 cal mol(-1) A(-2). To measure the hydrophobicity at the center, structures of an antigen-antibody complex where a buried phenylalanine was replaced by smaller hydrophobic residues were determined. By correlating structural changes with binding free energies, we estimate the hydrophobicity at this central site to be 46 cal mol(-1) A(-2), twice that at the periphery. This context dependence of the hydrophobic effect explains the clustering of hot spots at interface centers and has implications for hot spot prediction and the design of small molecule inhibitors.
Magnitude of the hydrophobic effect at central versus peripheral sites in protein-protein interfaces.,Li Y, Huang Y, Swaminathan CP, Smith-Gill SJ, Mariuzza RA Structure. 2005 Feb;13(2):297-307. PMID:15698573[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
- ↑ Li Y, Huang Y, Swaminathan CP, Smith-Gill SJ, Mariuzza RA. Magnitude of the hydrophobic effect at central versus peripheral sites in protein-protein interfaces. Structure. 2005 Feb;13(2):297-307. PMID:15698573 doi:10.1016/j.str.2004.12.012
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