4ooo: Difference between revisions
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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=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4oot|4oot]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4oot|4oot]]</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='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=4ooo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ooo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ooo RCSB], [http://www.ebi.ac.uk/pdbsum/4ooo PDBsum]</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=4ooo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ooo OCA], [http://pdbe.org/4ooo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ooo RCSB], [http://www.ebi.ac.uk/pdbsum/4ooo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ooo ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4ooo" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 00:53, 5 August 2016
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
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 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. References
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