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==X-ray structure of the lysozyme derivative of tetrakis(acetato)chlorido diruthenium(II,III) complex== | ==X-ray structure of the lysozyme derivative of tetrakis(acetato)chlorido diruthenium(II,III) complex== | ||
<StructureSection load='4ooo' size='340' side='right' caption='[[4ooo]], [[Resolution|resolution]] 2.15Å' scene=''> | <StructureSection load='4ooo' size='340' side='right'caption='[[4ooo]], [[Resolution|resolution]] 2.15Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ooo]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OOO OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4ooo]] 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=4OOO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OOO FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15Å</td></tr> | ||
<tr id=' | <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=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=RU0:TETRAKIS(ACETATO)CHLORIDODIRUTHENIUM(II,III)'>RU0</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=4ooo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ooo OCA], [https://pdbe.org/4ooo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ooo RCSB], [https://www.ebi.ac.uk/pdbsum/4ooo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ooo ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == 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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 20: | Line 19: | ||
</div> | </div> | ||
<div class="pdbe-citations 4ooo" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4ooo" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Lysozyme 3D structures|Lysozyme 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Gallus gallus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Merlino A]] | ||
Latest revision as of 20:17, 20 September 2023
X-ray structure of the lysozyme derivative of tetrakis(acetato)chlorido diruthenium(II,III) complexX-ray structure of the lysozyme derivative of tetrakis(acetato)chlorido diruthenium(II,III) complex
Structural highlights
FunctionLYSC_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 PubMedThe reaction between the paddle-wheel tetrakis(acetato)chloridodiruthenium(II,III) complex, [Ru2 (mu-O2 CCH3 )4 Cl] and hen egg-white lysozyme (HEWL) was investigated through ESI-MS and UV/Vis spectroscopy and the formation of a stable metal-protein adduct was unambiguously demonstrated. Remarkably, the diruthenium core is conserved in the adduct while two of the four acetate ligands are released. The crystal structure of this diruthenium-protein derivative was subsequently solved through X-ray diffraction analysis to 2.1 A resolution. The structural data are in agreement with the solution results. It was found that HEWL binds two diruthenium moieties, at Asp101 and Asp119, respectively, with the concomitant release of two acetate ligands from each diruthenium center. Unusual Structural Features in the Lysozyme Derivative of the Tetrakis(acetato)chloridodiruthenium(II,III) Complex.,Messori L, Marzo T, Sanches RN, Hanif-Ur-Rehman, de Oliveira Silva D, Merlino A Angew Chem Int Ed Engl. 2014 Jun 10;53(24):6172-5. doi: 10.1002/anie.201403337., Epub 2014 May 5. PMID:24796316[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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