9i8l: Difference between revisions

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'''Unreleased structure'''


The entry 9i8l is ON HOLD  until Paper Publication
==X-ray structure of a polyoxidovanadate/lysozyme adduct obtained when the protein is treated with [VIVO(acac)2</sub>] at 310 K==
<StructureSection load='9i8l' size='340' side='right'caption='[[9i8l]], [[Resolution|resolution]] 1.83&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9i8l]] 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=9I8L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9I8L FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.831&#8491;</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=NA:SODIUM+ION'>NA</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=9i8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9i8l OCA], [https://pdbe.org/9i8l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9i8l RCSB], [https://www.ebi.ac.uk/pdbsum/9i8l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9i8l ProSAT]</span></td></tr>
</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 ==
Crystals of the model protein lysozyme were grown and soaked with the potential drug V(IV)O(acetylacetonato)(2) at 37 degrees C. X-ray diffraction and electron paramagnetic resonance (EPR) data collected at this temperature reveal that mixed-valence cage-like polyoxidovanadate clusters are formed and covalently bind protein residue side chains at physiological temperature.


Authors: Tito, G., Ferraro, G., Merlino, A.
Formation of Mixed-Valence Cage-Like Polyoxidovanadates at 37 degrees C Upon Reaction of V(IV)O(acetylacetonato)(2) With Lysozyme.,Tito G, Ferraro G, Garribba E, Merlino A Chemistry. 2025 Apr 24:e202500488. doi: 10.1002/chem.202500488. PMID:40271720<ref>PMID:40271720</ref>


Description: X-ray structure of a polyoxidovanadate/lysozyme adduct obtained when the protein is treated with [VIVO(acac)2</sub>] at 310 K
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Tito, G]]
<div class="pdbe-citations 9i8l" style="background-color:#fffaf0;"></div>
[[Category: Ferraro, G]]
== References ==
[[Category: Merlino, A]]
<references/>
__TOC__
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Large Structures]]
[[Category: Ferraro G]]
[[Category: Merlino A]]
[[Category: Tito G]]
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