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| | <StructureSection load='4xyy' size='340' side='right'caption='[[4xyy]], [[Resolution|resolution]] 1.38Å' scene=''> | | <StructureSection load='4xyy' size='340' side='right'caption='[[4xyy]], [[Resolution|resolution]] 1.38Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4xyy]] 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=4XYY OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=4XYY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4xyy]] 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=4XYY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XYY FirstGlance]. <br> |
| | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EDN:ETHANE-1,2-DIAMINE'>EDN</scene>, <scene name='pdbligand=ZKG:ZIRCONIUM(IV)+PHOSPHOTUNGSTATE+KEGGIN'>ZKG</scene></td></tr> | | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EDN:ETHANE-1,2-DIAMINE'>EDN</scene>, <scene name='pdbligand=ZKG:ZIRCONIUM(IV)+PHOSPHOTUNGSTATE+KEGGIN'>ZKG</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=4xyy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xyy OCA], [https://pdbe.org/4xyy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xyy RCSB], [https://www.ebi.ac.uk/pdbsum/4xyy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xyy ProSAT]</span></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=4xyy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xyy OCA], [http://pdbe.org/4xyy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xyy RCSB], [http://www.ebi.ac.uk/pdbsum/4xyy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xyy 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: De Zitter E]] |
| - | [[Category: Meervelt, L Van]] | + | [[Category: Van Meervelt L]] |
| - | [[Category: Zitter, E De]]
| + | |
| - | [[Category: Co-crystallization]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Metalsubstituted polyoxometalate]]
| + | |
| 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
Successful co-crystallization of a noncovalent complex between hen egg-white lysozyme (HEWL) and the monomeric ZrIV -substituted Keggin polyoxometalate (POM) (Zr1 K1), (Et2 NH2 )3 [Zr(PW11 O39 )] (1), has been achieved, and its single-crystal X-ray structure has been determined. The dimeric ZrIV -substituted Keggin-type polyoxometalate (Zr1 K2), (Et2 NH2 )10 [Zr(PW11 O39 )2 ] (2), has been previously shown to exhibit remarkable selectivity towards HEWL hydrolysis. The reported X-ray structure shows that the hydrolytically active ZrIV -substituted Keggin POM exists as a monomeric species. Prior to hydrolysis, this monomer interacts with HEWL in the vicinity of the previously identified cleavage sites found at Trp28-Val29 and Asn44-Arg45, through water-mediated H-bonding and electrostatic interactions. Three binding sites are observed at the interface of the negatively charged Keggin POM and the positively charged regions of HEWL at: 1) Gly16, Tyr20, and Arg21; 2) Asn44, Arg45, and Asn46; and 3) Arg128.
Structural Characterization of the Complex between Hen Egg-White Lysozyme and Zr -Substituted Keggin Polyoxometalate as Artificial Protease.,Sap A, De Zitter E, Van Meervelt L, Parac-Vogt TN Chemistry. 2015 Jul 14. doi: 10.1002/chem.201501998. PMID:26179600[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
- ↑ Sap A, De Zitter E, Van Meervelt L, Parac-Vogt TN. Structural Characterization of the Complex between Hen Egg-White Lysozyme and Zr -Substituted Keggin Polyoxometalate as Artificial Protease. Chemistry. 2015 Jul 14. doi: 10.1002/chem.201501998. PMID:26179600 doi:http://dx.doi.org/10.1002/chem.201501998
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