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| | <StructureSection load='2aub' size='340' side='right'caption='[[2aub]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='2aub' size='340' side='right'caption='[[2aub]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2aub]] 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=2AUB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AUB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2aub]] 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=2AUB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AUB 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 diffraction, [[Resolution|Resolution]] 1.7Å</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=2aub FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aub OCA], [http://pdbe.org/2aub PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2aub RCSB], [http://www.ebi.ac.uk/pdbsum/2aub PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2aub 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=2aub FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aub OCA], [https://pdbe.org/2aub PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2aub RCSB], [https://www.ebi.ac.uk/pdbsum/2aub PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2aub 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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| | [[Category: Gallus gallus]] | | [[Category: Gallus gallus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lysozyme]]
| + | [[Category: Fiordoro S]] |
| - | [[Category: Fiordoro, S]] | + | [[Category: Nicolini C]] |
| - | [[Category: Nicolini, C]] | + | [[Category: Pechkova E]] |
| - | [[Category: Pechkova, E]] | + | [[Category: Sivozhelezov V]] |
| - | [[Category: Sivozhelezov, V]] | + | [[Category: Tropiano G]] |
| - | [[Category: Tropiano, G]] | + | |
| - | [[Category: Hydrolase]]
| + | |
| 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
The present report is dedicated to a systematic comparison of crystal structures produced by the nanobiofilm template method and by the classical hanging-drop vapour-diffusion method. Crystals grown by the innovative nanostructured template method appear indeed radiation-resistant even in the presence of a third-generation highly focused beam at the European Synchrotron Radiation Facility. The implications of this finding for protein crystallography are discussed here in terms of water redistribution and of the detailed atomic resolution comparative studies of the two crystal structures with or without nanobiofilm template, as emerging also from circular-dichroism and thermal denaturation studies.
Comparison of lysozyme structures derived from thin-film-based and classical crystals.,Pechkova E, Sivozhelezov V, Tropiano G, Fiordoro S, Nicolini C Acta Crystallogr D Biol Crystallogr. 2005 Jun;61(Pt 6):803-8. Epub 2005, May 26. PMID:15930644[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
- ↑ Pechkova E, Sivozhelezov V, Tropiano G, Fiordoro S, Nicolini C. Comparison of lysozyme structures derived from thin-film-based and classical crystals. Acta Crystallogr D Biol Crystallogr. 2005 Jun;61(Pt 6):803-8. Epub 2005, May 26. PMID:15930644 doi:10.1107/S0907444905006578
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