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| | <StructureSection load='5a3z' size='340' side='right'caption='[[5a3z]], [[Resolution|resolution]] 1.59Å' scene=''> | | <StructureSection load='5a3z' size='340' side='right'caption='[[5a3z]], [[Resolution|resolution]] 1.59Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5a3z]] 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=5A3Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A3Z FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5a3z]] 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=5A3Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A3Z FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5a3y|5a3y]]</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=5a3z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a3z OCA], [https://pdbe.org/5a3z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a3z RCSB], [https://www.ebi.ac.uk/pdbsum/5a3z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a3z ProSAT]</span></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='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=5a3z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a3z OCA], [http://pdbe.org/5a3z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5a3z RCSB], [http://www.ebi.ac.uk/pdbsum/5a3z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5a3z 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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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Line 27: |
| | [[Category: Gallus gallus]] | | [[Category: Gallus gallus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lysozyme]]
| + | [[Category: Bourenkov G]] |
| - | [[Category: Bourenkov, G]] | + | [[Category: Gordeliy VI]] |
| - | [[Category: Gordeliy, V I]] | + | [[Category: Leonard GA]] |
| - | [[Category: Leonard, G A]] | + | [[Category: McCarthy AA]] |
| - | [[Category: McCarthy, A A]] | + | [[Category: Mueller-Dieckmann C]] |
| - | [[Category: Mueller-Dieckmann, C]] | + | [[Category: Popov AN]] |
| - | [[Category: Popov, A N]] | + | [[Category: Round ES]] |
| - | [[Category: Round, E S]] | + | [[Category: Svensson O]] |
| - | [[Category: Sanctis, D de]]
| + | [[Category: Zander U]] |
| - | [[Category: Svensson, O]] | + | [[Category: De Sanctis D]] |
| - | [[Category: Zander, U]] | + | |
| - | [[Category: Hydrolase]] | + | |
| - | [[Category: Multi crystal data collection]]
| + | |
| - | [[Category: Ssx]]
| + | |
| - | [[Category: Synchrotron serial crystallography]]
| + | |
| 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
Here, an automated procedure is described to identify the positions of many cryocooled crystals mounted on the same sample holder, to rapidly predict and rank their relative diffraction strengths and to collect partial X-ray diffraction data sets from as many of the crystals as desired. Subsequent hierarchical cluster analysis then allows the best combination of partial data sets, optimizing the quality of the final data set obtained. The results of applying the method developed to various systems and scenarios including the compilation of a complete data set from tiny crystals of the membrane protein bacteriorhodopsin and the collection of data sets for successful structure determination using the single-wavelength anomalous dispersion technique are also presented.
MeshAndCollect: an automated multi-crystal data-collection workflow for synchrotron macromolecular crystallography beamlines.,Zander U, Bourenkov G, Popov AN, de Sanctis D, Svensson O, McCarthy AA, Round E, Gordeliy V, Mueller-Dieckmann C, Leonard GA Acta Crystallogr D Biol Crystallogr. 2015 Nov 1;71(Pt 11):2328-43. doi:, 10.1107/S1399004715017927. Epub 2015 Oct 31. PMID:26527148[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
- ↑ Zander U, Bourenkov G, Popov AN, de Sanctis D, Svensson O, McCarthy AA, Round E, Gordeliy V, Mueller-Dieckmann C, Leonard GA. MeshAndCollect: an automated multi-crystal data-collection workflow for synchrotron macromolecular crystallography beamlines. Acta Crystallogr D Biol Crystallogr. 2015 Nov 1;71(Pt 11):2328-43. doi:, 10.1107/S1399004715017927. Epub 2015 Oct 31. PMID:26527148 doi:http://dx.doi.org/10.1107/S1399004715017927
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