|
|
| (3 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==ORTHORHOMBIC LYSOZYME CRYSTALLIZED AT HIGH TEMPERATURE (310K)== | | ==ORTHORHOMBIC LYSOZYME CRYSTALLIZED AT HIGH TEMPERATURE (310K)== |
| - | <StructureSection load='1bgi' size='340' side='right' caption='[[1bgi]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='1bgi' size='340' side='right'caption='[[1bgi]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1bgi]] 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=1BGI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BGI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1bgi]] 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=1BGI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BGI FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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]] 1.7Å</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=CL:CHLORIDE+ION'>CL</scene></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=1bgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bgi OCA], [http://pdbe.org/1bgi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bgi RCSB], [http://www.ebi.ac.uk/pdbsum/1bgi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bgi 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=1bgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bgi OCA], [https://pdbe.org/1bgi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bgi RCSB], [https://www.ebi.ac.uk/pdbsum/1bgi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bgi 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]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bg/1bgi_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bg/1bgi_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> |
| Line 37: |
Line 37: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Gallus gallus]] | | [[Category: Gallus gallus]] |
| - | [[Category: Lysozyme]] | + | [[Category: Large Structures]] |
| - | [[Category: Chernov, A A]] | + | [[Category: Chernov AA]] |
| - | [[Category: Komatsu, H]] | + | [[Category: Komatsu H]] |
| - | [[Category: Matsuura, Y]] | + | [[Category: Matsuura Y]] |
| - | [[Category: Oki, H]] | + | [[Category: Oki H]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: O-glycosyl]]
| + | |
| 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
The structure of orthorhombic hen egg-white lysozyme (HEWL) crystallized at 310 K has been refined at 1.7 A resolution. Large displacements of the side-chain atoms with respect to the tetragonal structure were observed in many places, in contrast to small displacements of the main-chain atoms. A chloride-ion binding site was observed at an interface of two molecules, but at a different position to the binding site in the tetragonal form. The analysis of intermolecular contacts in the crystal has shown the presence of three independent intermolecular contacts which are called macrobonds A, B and C. Arginine side chains are frequently involved in these macrobonds, suggesting that the high frequency of this residue in HEWL may be a possible reason for the multiple polymorphs of this protein. The crystal forms were determined using a light-reflecting device on a four-circle diffractometer. Correlations between crystal forms and the three-dimensional macrobond networks were interpreted in terms of their components in various crystallographic planes, making use of approximate strengths of hydrogen-bond and van der Waals interatomic forces.
Refined structure of orthorhombic lysozyme crystallized at high temperature: correlation between morphology and intermolecular contacts.,Oki H, Matsuura Y, Komatsu H, Chernov AA Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):114-21. Epub 1999, Jan 1. PMID:10089401[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
- ↑ Oki H, Matsuura Y, Komatsu H, Chernov AA. Refined structure of orthorhombic lysozyme crystallized at high temperature: correlation between morphology and intermolecular contacts. Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):114-21. Epub 1999, Jan 1. PMID:10089401 doi:10.1107/S0907444998008713
|
