8rny
From Proteopedia
(Difference between revisions)
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==Hen Egg White Lysozyme soaked with with [H2Ind][trans-RuCl4(DMSO)(HInd)]== | ==Hen Egg White Lysozyme soaked with with [H2Ind][trans-RuCl4(DMSO)(HInd)]== | ||
| - | <StructureSection load='8rny' size='340' side='right'caption='[[8rny]]' scene=''> | + | <StructureSection load='8rny' size='340' side='right'caption='[[8rny]], [[Resolution|resolution]] 1.02Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8RNY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8RNY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[8rny]] 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=8RNY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8RNY FirstGlance]. <br> |
| - | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction</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]] 1.02Å</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>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=RU:RUTHENIUM+ION'>RU</scene></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=8rny FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8rny OCA], [https://pdbe.org/8rny PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8rny RCSB], [https://www.ebi.ac.uk/pdbsum/8rny PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8rny 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=8rny FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8rny OCA], [https://pdbe.org/8rny PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8rny RCSB], [https://www.ebi.ac.uk/pdbsum/8rny PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8rny ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [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;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | This study presents a comprehensive structural analysis of the adducts formed upon the reaction of two Ru(III) complexes [HIsq][trans-Ru(III)Cl(4)(dmso)(Isq)] (1) and [H(2)Ind][trans-Ru(III)Cl(4)(dmso)(HInd)] (2) (where HInd-indazole, Isq-isoquinoline, analogs of NAMI-A) and two Ru(II) complexes, cis-[RuCl(2)(dmso)(4)] (c) and trans-[RuCl(2)(dmso)(4)] (t), with hen-egg white lysozyme (HEWL). Additionally, the crystal structure of an adduct of human lysozyme (HL) with ruthenium complex, [H(2)Ind][trans-RuCl(4)(dmso)(HInd)] was solved. X-ray crystallographic data analysis revealed that all studied Ru complexes, regardless of coordination surroundings and metal center charge, coordinate to the same amino acids (His15, Arg14, and Asp101) of HEWL, losing most of their original ligands. In the case of the 2-HL adduct, two distinct metalation sites: (i) Arg107, Arg113 and (ii) Gln127, Gln129, were identified. Crystallographic data were supported by studies of the interaction of 1 and 2 with HEWL in an aqueous solution. Hydrolytic stability studies revealed that both complexes 1 and 2 liberate the N-heterocyclic ligand under crystallization-like conditions (pH 4.5) as well as under physiological pH conditions, and this process is not significantly affected by the presence of HEWL. A comparative examination of nine crystal structures of Ru complexes with lysozyme, obtained through soaking and co-crystallization experiments, together with in-solution studies of the interaction between 1 and 2 with HEWL, indicates that the hydrolytic release of the N-heterocyclic ligand is one of the critical factors in the interaction between Ru complexes and lysozyme. This understanding is crucial in shedding light on the tendency of Ru complexes to target diverse metalation sites during the formation and in the final forms of the adducts with proteins. | ||
| + | |||
| + | Exploring the coordination chemistry of ruthenium complexes with lysozymes: structural and in-solution studies.,Oszajca M, Flejszar M, Szura A, Drozdz P, Brindell M, Kurpiewska K Front Chem. 2024 Apr 4;12:1371637. doi: 10.3389/fchem.2024.1371637. eCollection , 2024. PMID:38638879<ref>PMID:38638879</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8rny" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Gallus gallus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Brindell M]] |
| + | [[Category: Drozdz P]] | ||
| + | [[Category: Flejszar M]] | ||
| + | [[Category: Kurpiewska K]] | ||
| + | [[Category: Oszajca M]] | ||
| + | [[Category: Szura A]] | ||
Current revision
Hen Egg White Lysozyme soaked with with [H2Ind][trans-RuCl4(DMSO)(HInd)]
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