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| | <StructureSection load='5hnc' size='340' side='right'caption='[[5hnc]], [[Resolution|resolution]] 1.76Å' scene=''> | | <StructureSection load='5hnc' size='340' side='right'caption='[[5hnc]], [[Resolution|resolution]] 1.76Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5hnc]] 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=5HNC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HNC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5hnc]] 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=5HNC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HNC 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]] 1.76Å</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=5hnc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hnc OCA], [http://pdbe.org/5hnc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hnc RCSB], [http://www.ebi.ac.uk/pdbsum/5hnc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hnc 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=5hnc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hnc OCA], [https://pdbe.org/5hnc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hnc RCSB], [https://www.ebi.ac.uk/pdbsum/5hnc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hnc 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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| | [[Category: Gallus gallus]] | | [[Category: Gallus gallus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lysozyme]]
| + | [[Category: Baba S]] |
| - | [[Category: Baba, S]] | + | [[Category: Kimura F]] |
| - | [[Category: Kimura, F]] | + | [[Category: Kimura T]] |
| - | [[Category: Kimura, T]] | + | [[Category: Kusaka K]] |
| - | [[Category: Kusaka, K]] | + | [[Category: Mizuno N]] |
| - | [[Category: Mizuno, N]] | + | [[Category: Tsukui S]] |
| - | [[Category: Tsukui, S]] | + | |
| - | [[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]
Publication Abstract from PubMed
Protein microcrystals magnetically aligned in D2O hydrogels were subjected to neutron diffraction measurements, and reflections were observed for the first time to a resolution of 3.4 A from lysozyme microcrystals ( approximately 10 x 10 x 50 microm). This result demonstrated the possibility that magnetically oriented microcrystals consolidated in D2O gels may provide a promising means to obtain single-crystal neutron diffraction from proteins that do not crystallize at the sizes required for neutron diffraction structure determination. In addition, lysozyme microcrystals aligned in H2O hydrogels allowed structure determination at a resolution of 1.76 A at room temperature by X-ray diffraction. The use of gels has advantages since the microcrystals are measured under hydrated conditions.
Neutron and X-ray single-crystal diffraction from protein microcrystals via magnetically oriented microcrystal arrays in gels.,Tsukui S, Kimura F, Kusaka K, Baba S, Mizuno N, Kimura T Acta Crystallogr D Struct Biol. 2016 Jul 1;72(Pt 7):823-9. doi:, 10.1107/S2059798316007415. Epub 2016 Jun 23. PMID:27377379[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
- ↑ Tsukui S, Kimura F, Kusaka K, Baba S, Mizuno N, Kimura T. Neutron and X-ray single-crystal diffraction from protein microcrystals via magnetically oriented microcrystal arrays in gels. Acta Crystallogr D Struct Biol. 2016 Jul 1;72(Pt 7):823-9. doi:, 10.1107/S2059798316007415. Epub 2016 Jun 23. PMID:27377379 doi:http://dx.doi.org/10.1107/S2059798316007415
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