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| | <StructureSection load='4nhs' size='340' side='right'caption='[[4nhs]], [[Resolution|resolution]] 1.99Å' scene=''> | | <StructureSection load='4nhs' size='340' side='right'caption='[[4nhs]], [[Resolution|resolution]] 1.99Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4nhs]] 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=4NHS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NHS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4nhs]] 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=4NHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NHS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2T8:CARBONYL(TETRACHLORO)OXIDOIRIDIUM'>2T8</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.99Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4n9r|4n9r]], [[4nhp|4nhp]], [[4nhq|4nhq]], [[4nht|4nht]], [[4nij|4nij]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2T8:CARBONYL(TETRACHLORO)OXIDOIRIDIUM'>2T8</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=4nhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nhs OCA], [https://pdbe.org/4nhs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nhs RCSB], [https://www.ebi.ac.uk/pdbsum/4nhs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nhs ProSAT]</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=4nhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nhs OCA], [http://pdbe.org/4nhs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nhs RCSB], [http://www.ebi.ac.uk/pdbsum/4nhs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nhs 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: Bikiel DE]] |
| - | [[Category: Bikiel, D E]] | + | [[Category: Merlino A]] |
| - | [[Category: Merlino, A]] | + | [[Category: Petruk AA]] |
| - | [[Category: Petruk, A A]] | + | [[Category: Vergara A]] |
| - | [[Category: Vergara, A]] | + | |
| - | [[Category: Bacterial cell wall]]
| + | |
| - | [[Category: C-type]]
| + | |
| - | [[Category: C-type lysozyme/alpha-lactalbumin family]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Peptidoglycan]]
| + | |
| 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
Carbon monoxide releasing molecules (CORMs) have important bactericidal, anti-inflammatory, neuroprotective, and antiapoptotic effects and can be used as tools for CO physiology experiments, including studies on vasodilation. In this context, a new class of CO releasing molecules, based on pentachlorocarbonyliridate(III) derivative have been recently reported. Although there is a growing interest in the characterization of protein-CORMs interactions, only limited structural information on CORM binding to protein and CO release has been available to date. Here, we report six different crystal structures describing events ranging from CORM entrance into the protein crystal up to the CO release and a biophysical characterization by isothermal titration calorimetry, Raman microspectroscopy, and molecular dynamics simulations of the complex between a pentachlorocarbonyliridate(III) derivative and hen egg white lysozyme, a model protein. Altogether, the data indicate the formation of a complex in which the ligand can bind to different sites of the protein surface and provide clues on the mechanism of adduct formation and CO release.
Interaction between proteins and Ir based CO releasing molecules: mechanism of adduct formation and CO release.,Petruk AA, Vergara A, Marasco D, Bikiel D, Doctorovich F, Estrin DA, Merlino A Inorg Chem. 2014 Oct 6;53(19):10456-62. doi: 10.1021/ic501498g. Epub 2014 Sep 12. PMID:25215611[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
- ↑ Petruk AA, Vergara A, Marasco D, Bikiel D, Doctorovich F, Estrin DA, Merlino A. Interaction between proteins and Ir based CO releasing molecules: mechanism of adduct formation and CO release. Inorg Chem. 2014 Oct 6;53(19):10456-62. doi: 10.1021/ic501498g. Epub 2014 Sep 12. PMID:25215611 doi:http://dx.doi.org/10.1021/ic501498g
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