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| | <StructureSection load='4g49' size='340' side='right'caption='[[4g49]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='4g49' size='340' side='right'caption='[[4g49]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4g49]] 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=4G49 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G49 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4g49]] 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=4G49 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G49 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CPT:CISPLATIN'>CPT</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CPT:CISPLATIN'>CPT</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4dd0|4dd0]], [[4dd1|4dd1]], [[4dd2|4dd2]], [[4dd3|4dd3]], [[4dd4|4dd4]], [[4dd6|4dd6]], [[4dd7|4dd7]], [[4dd9|4dd9]], [[4dda|4dda]], [[4ddb|4ddb]], [[4ddc|4ddc]], [[4g4a|4g4a]], [[4g4b|4g4b]], [[4g4c|4g4c]], [[4g4h|4g4h]]</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=4g49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g49 OCA], [https://pdbe.org/4g49 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g49 RCSB], [https://www.ebi.ac.uk/pdbsum/4g49 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g49 ProSAT]</span></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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4g49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g49 OCA], [http://pdbe.org/4g49 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4g49 RCSB], [http://www.ebi.ac.uk/pdbsum/4g49 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4g49 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: Helliwell JR]] |
| - | [[Category: Helliwell, J R]] | + | [[Category: Kroon-Batenburg LMJ]] |
| - | [[Category: Kroon-Batenburg, L M.J]] | + | [[Category: Schreurs AMM]] |
| - | [[Category: Schreurs, A M.M]] | + | [[Category: Tanley SWM]] |
| - | [[Category: Tanley, S W.M]] | + | |
| - | [[Category: Aqueous media]]
| + | |
| - | [[Category: Capillary]]
| + | |
| - | [[Category: Carboplatin]]
| + | |
| - | [[Category: Cisplatin]]
| + | |
| - | [[Category: Dmso media]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Omega scan data collection]]
| + | |
| 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
The anticancer complexes cisplatin and carboplatin are known to bind to both the Ndelta and the N atoms of His15 of hen egg-white lysozyme (HEWL) in the presence of dimethyl sulfoxide (DMSO). However, neither binds in aqueous media after 4 d of crystallization and crystal growth, suggesting that DMSO facilitates cisplatin/carboplatin binding to the N atoms of His15 by an unknown mechanism. Crystals of HEWL cocrystallized with cisplatin in both aqueous and DMSO media, of HEWL cocrystallized with carboplatin in DMSO medium and of HEWL cocrystallized with cisplatin and N-acetylglucosamine (NAG) in DMSO medium were stored for between seven and 15 months. X-ray diffraction studies of these crystals were carried out on a Bruker APEX II home-source diffractometer at room temperature. Room-temperature X-ray diffraction data collection removed the need for cryoprotectants to be used, ruling out any effect that the cryoprotectants might have had on binding to the protein. Both cisplatin and carboplatin still bind to both the Ndelta and N atoms of His15 in DMSO media as expected, but more detail for the cyclobutanedicarboxylate (CBDC) moiety of carboplatin was observed at the N binding site. However, two molecules of cisplatin were now observed to be bound to His15 in aqueous conditions. The platinum peak positions were identified using anomalous difference electron-density maps as a cross-check with Fo-Fc OMIT electron-density maps. The occupancies of each binding site were calculated using SHELXTL. These results show that over time cisplatin binds to both N atoms of His15 of HEWL in aqueous media, whereas this binding is speeded up in the presence of DMSO. The implication of cisplatin binding to proteins after a prolonged period of time is an important consideration for the length of treatment in patients who are given cisplatin.
Room-temperature X-ray diffraction studies of cisplatin and carboplatin binding to His15 of HEWL after prolonged chemical exposure.,Tanley SW, Schreurs AM, Kroon-Batenburg LM, Helliwell JR Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Nov 1;68(Pt 11):1300-6., doi: 10.1107/S1744309112042005. Epub 2012 Oct 26. PMID:23143236[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
- ↑ Tanley SW, Schreurs AM, Kroon-Batenburg LM, Helliwell JR. Room-temperature X-ray diffraction studies of cisplatin and carboplatin binding to His15 of HEWL after prolonged chemical exposure. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Nov 1;68(Pt 11):1300-6., doi: 10.1107/S1744309112042005. Epub 2012 Oct 26. PMID:23143236 doi:http://dx.doi.org/10.1107/S1744309112042005
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