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| <StructureSection load='5ocv' size='340' side='right'caption='[[5ocv]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='5ocv' size='340' side='right'caption='[[5ocv]], [[Resolution|resolution]] 2.20Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[5ocv]] 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=5OCV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5OCV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ocv]] 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=5OCV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OCV FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron crystallography, [[Resolution|Resolution]] 2.2Å</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=NA:SODIUM+ION'>NA</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=5ocv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ocv OCA], [http://pdbe.org/5ocv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ocv RCSB], [http://www.ebi.ac.uk/pdbsum/5ocv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ocv 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=5ocv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ocv OCA], [https://pdbe.org/5ocv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ocv RCSB], [https://www.ebi.ac.uk/pdbsum/5ocv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ocv 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: Hogbom M]] |
- | [[Category: Hogbom, M]] | + | [[Category: Hovmoller S]] |
- | [[Category: Hovmoller, S]] | + | [[Category: Lebrette H]] |
- | [[Category: Lebrette, H]] | + | [[Category: Srinivas V]] |
- | [[Category: Srinivas, V]] | + | [[Category: Xu H]] |
- | [[Category: Xu, H]] | + | [[Category: Yang T]] |
- | [[Category: Yang, T]] | + | [[Category: Zou X]] |
- | [[Category: Zou, X]] | + | |
- | [[Category: Hydrolase]]
| + | |
- | [[Category: Lysozyme activity]]
| + | |
| 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
Recent developments of novel electron diffraction techniques have shown to be powerful for determination of atomic resolution structures from micron- and nano-sized crystals, too small to be studied by single-crystal X-ray diffraction. In this work, the structure of a rare lysozyme polymorph is solved and refined using continuous rotation MicroED data and standard X-ray crystallographic software. Data collection was performed on a standard 200 kV transmission electron microscope (TEM) using a highly sensitive detector with a short readout time. The data collection is fast ( approximately 3 min per crystal), allowing multiple datasets to be rapidly collected from a large number of crystals. We show that merging data from 33 crystals significantly improves not only the data completeness, overall I/sigma and the data redundancy, but also the quality of the final atomic model. This is extremely useful for electron beam-sensitive crystals of low symmetry or with a preferred orientation on the TEM grid.
A Rare Lysozyme Crystal Form Solved Using Highly Redundant Multiple Electron Diffraction Datasets from Micron-Sized Crystals.,Xu H, Lebrette H, Yang T, Srinivas V, Hovmoller S, Hogbom M, Zou X Structure. 2018 Mar 1. pii: S0969-2126(18)30055-8. doi:, 10.1016/j.str.2018.02.015. PMID:29551291[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
- ↑ Xu H, Lebrette H, Yang T, Srinivas V, Hovmoller S, Hogbom M, Zou X. A Rare Lysozyme Crystal Form Solved Using Highly Redundant Multiple Electron Diffraction Datasets from Micron-Sized Crystals. Structure. 2018 Mar 1. pii: S0969-2126(18)30055-8. doi:, 10.1016/j.str.2018.02.015. PMID:29551291 doi:http://dx.doi.org/10.1016/j.str.2018.02.015
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