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| | <StructureSection load='1lzt' size='340' side='right'caption='[[1lzt]], [[Resolution|resolution]] 1.97Å' scene=''> | | <StructureSection load='1lzt' size='340' side='right'caption='[[1lzt]], [[Resolution|resolution]] 1.97Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1lzt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LZT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LZT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1lzt]] 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=1LZT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LZT 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]] 1.97Å</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=1lzt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lzt OCA], [http://pdbe.org/1lzt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lzt RCSB], [http://www.ebi.ac.uk/pdbsum/1lzt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lzt 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=1lzt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lzt OCA], [https://pdbe.org/1lzt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lzt RCSB], [https://www.ebi.ac.uk/pdbsum/1lzt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lzt 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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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lz/1lzt_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lz/1lzt_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chick]] | + | [[Category: Gallus gallus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lysozyme]]
| + | [[Category: Brown GM]] |
| - | [[Category: Brown, G M]] | + | [[Category: Hodsdon JM]] |
| - | [[Category: Hodsdon, J M]] | + | [[Category: Jensen LH]] |
| - | [[Category: Jensen, L H]] | + | [[Category: Sieker LC]] |
| - | [[Category: Sieker, L C]] | + | |
| 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
X-ray diffraction data to 1.5 A resolution have been collected for triclinic crystals of hen egg white lysozyme. The triclinic model was derived from the tetragonal one by the rotation function and refined initially by Fo-Fc and differential difference syntheses against 2 A resolution data. Refinement was continued by differential difference cycles against the 1.5 A data until R was reduced to 0.220. Although the initial refinement was rapid, it was subsequently a matter of attrition, leading to a complete recheck of the data and the discovery of systematic error which affected primarily the high-resolution data. Refinement was continued against the corrected 2 A data by block-diagonal least squares. After five cycles the refinement was terminated at R = 0.254 because of the imminent availability of a preferred refinement program. Problems with the protein model, the solvent, and the interaction of the scale and thermal parameters are discussed. The experiences gained in this study are summarized.
Refinement of triclinic lysozyme: I. Fourier and least-squares methods.,Hodsdon JM, Brown GM, Sieker LC, Jensen LH Acta Crystallogr B. 1990 Feb 1;46 ( Pt 1):54-62. PMID:2302326[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
- ↑ Hodsdon JM, Brown GM, Sieker LC, Jensen LH. Refinement of triclinic lysozyme: I. Fourier and least-squares methods. Acta Crystallogr B. 1990 Feb 1;46 ( Pt 1):54-62. PMID:2302326
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