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| | <StructureSection load='5o4x' size='340' side='right'caption='[[5o4x]], [[Resolution|resolution]] 2.11Å' scene=''> | | <StructureSection load='5o4x' size='340' side='right'caption='[[5o4x]], [[Resolution|resolution]] 2.11Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5o4x]] 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=5O4X OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5O4X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5o4x]] 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=5O4X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5O4X 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">Electron crystallography, [[Resolution|Resolution]] 2.11Å</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=5o4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o4x OCA], [http://pdbe.org/5o4x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5o4x RCSB], [http://www.ebi.ac.uk/pdbsum/5o4x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5o4x 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=5o4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o4x OCA], [https://pdbe.org/5o4x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5o4x RCSB], [https://www.ebi.ac.uk/pdbsum/5o4x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5o4x 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: Abrahams JP]] |
| - | [[Category: Abrahams, J P]] | + | [[Category: Clabbers MTB]] |
| - | [[Category: Clabbers, M T.B]] | + | [[Category: Gruene T]] |
| - | [[Category: Genderen, E van]]
| + | [[Category: Wan W]] |
| - | [[Category: Gruene, T]] | + | [[Category: Wiegers EL]] |
| - | [[Category: Wan, W]] | + | [[Category: Van Genderen E]] |
| - | [[Category: Wiegers, E L]] | + | |
| - | [[Category: Hydrolase]] | + | |
| - | [[Category: Nanocrystal]]
| + | |
| 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
Three-dimensional nanometre-sized crystals of macromolecules currently resist structure elucidation by single-crystal X-ray crystallography. Here, a single nanocrystal with a diffracting volume of only 0.14 microm3, i.e. no more than 6 x 105 unit cells, provided sufficient information to determine the structure of a rare dimeric polymorph of hen egg-white lysozyme by electron crystallography. This is at least an order of magnitude smaller than was previously possible. The molecular-replacement solution, based on a monomeric polyalanine model, provided sufficient phasing power to show side-chain density, and automated model building was used to reconstruct the side chains. Diffraction data were acquired using the rotation method with parallel beam diffraction on a Titan Krios transmission electron microscope equipped with a novel in-house-designed 1024 x 1024 pixel Timepix hybrid pixel detector for low-dose diffraction data collection. Favourable detector characteristics include the ability to accurately discriminate single high-energy electrons from X-rays and count them, fast readout to finely sample reciprocal space and a high dynamic range. This work, together with other recent milestones, suggests that electron crystallography can provide an attractive alternative in determining biological structures.
Protein structure determination by electron diffraction using a single three-dimensional nanocrystal.,Clabbers MTB, van Genderen E, Wan W, Wiegers EL, Gruene T, Abrahams JP Acta Crystallogr D Struct Biol. 2017 Sep 1;73(Pt 9):738-748. doi:, 10.1107/S2059798317010348. Epub 2017 Aug 15. PMID:28876237[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
- ↑ Clabbers MTB, van Genderen E, Wan W, Wiegers EL, Gruene T, Abrahams JP. Protein structure determination by electron diffraction using a single three-dimensional nanocrystal. Acta Crystallogr D Struct Biol. 2017 Sep 1;73(Pt 9):738-748. doi:, 10.1107/S2059798317010348. Epub 2017 Aug 15. PMID:28876237 doi:http://dx.doi.org/10.1107/S2059798317010348
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