8om8: Difference between revisions
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The | ==X-ray structure of lysozyme obtained upon reaction with [VIVO(empp)2] (Structure A)== | ||
<StructureSection load='8om8' size='340' side='right'caption='[[8om8]], [[Resolution|resolution]] 1.08Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8om8]] 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=8OM8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8OM8 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=VSU:tris-[(1-methyl-2-ethyl-3-hydroxy-4(1H)-pyridinone)]-V(V)3O7'>VSU</scene>, <scene name='pdbligand=VTZ:1-methyl-2-ethyl-3-hydroxy-4(1H)-pyridinone)V(IV)O4'>VTZ</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=8om8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8om8 OCA], [https://pdbe.org/8om8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8om8 RCSB], [https://www.ebi.ac.uk/pdbsum/8om8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8om8 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 == | |||
Vanadium complexes (VCs) are promising agents for the treatment, among others, of diabetes and cancer. The development of vanadium-based drugs is mainly limited by a scarce knowledge of the active species in the target organs, which is often determined by the interaction of VCs with biological macromolecules like proteins. Here, we have studied the binding of [V(IV)O(empp)(2)] (where Hempp is 1-methyl-2-ethyl-3-hydroxy-4(1H)-pyridinone), an antidiabetic and anticancer VC, with the model protein hen egg white lysozyme (HEWL) by electrospray ionization-mass spectrometry (ESI-MS), electron paramagnetic resonance (EPR), and X-ray crystallography. ESI-MS and EPR techniques reveal that, in aqueous solution, both the species [V(IV)O(empp)(2)] and [V(IV)O(empp)(H(2)O)](+), derived from the first one upon the loss of a empp(-) ligand, interact with HEWL. Crystallographic data, collected under different experimental conditions, show covalent binding of [V(IV)O(empp)(H(2)O)](+) to the side chain of Asp48, and noncovalent binding of cis-[V(IV)O(empp)(2)(H(2)O)], [V(IV)O(empp)(H(2)O)](+), [V(IV)O(empp)(H(2)O)(2)](+), and of an unusual trinuclear oxidovanadium(V) complex, [V(V)(3)O(6)(empp)(3)(H(2)O)], with accessible sites on the protein surface. The possibility of covalent and noncovalent binding with different strength and of interaction with various sites favor the formation of adducts with the multiple binding of vanadium moieties, allowing the transport in blood and cellular fluids of more than one metal-containing species with a possible amplification of the biological effects. | |||
Implications of Protein Interaction in the Speciation of Potential V(IV)O-Pyridinone Drugs.,Ferraro G, Paolillo M, Sciortino G, Pisanu F, Garribba E, Merlino A Inorg Chem. 2023 May 29;62(21):8407-8417. doi: 10.1021/acs.inorgchem.3c01041. , Epub 2023 May 17. PMID:37195003<ref>PMID:37195003</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Ferraro | <div class="pdbe-citations 8om8" style="background-color:#fffaf0;"></div> | ||
[[Category: Merlino | == References == | ||
[[Category: Paolillo | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Gallus gallus]] | |||
[[Category: Large Structures]] | |||
[[Category: Ferraro G]] | |||
[[Category: Merlino A]] | |||
[[Category: Paolillo M]] | |||
Latest revision as of 08:43, 7 June 2023
X-ray structure of lysozyme obtained upon reaction with [VIVO(empp)2] (Structure A)X-ray structure of lysozyme obtained upon reaction with [VIVO(empp)2] (Structure A)
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 PubMedVanadium complexes (VCs) are promising agents for the treatment, among others, of diabetes and cancer. The development of vanadium-based drugs is mainly limited by a scarce knowledge of the active species in the target organs, which is often determined by the interaction of VCs with biological macromolecules like proteins. Here, we have studied the binding of [V(IV)O(empp)(2)] (where Hempp is 1-methyl-2-ethyl-3-hydroxy-4(1H)-pyridinone), an antidiabetic and anticancer VC, with the model protein hen egg white lysozyme (HEWL) by electrospray ionization-mass spectrometry (ESI-MS), electron paramagnetic resonance (EPR), and X-ray crystallography. ESI-MS and EPR techniques reveal that, in aqueous solution, both the species [V(IV)O(empp)(2)] and [V(IV)O(empp)(H(2)O)](+), derived from the first one upon the loss of a empp(-) ligand, interact with HEWL. Crystallographic data, collected under different experimental conditions, show covalent binding of [V(IV)O(empp)(H(2)O)](+) to the side chain of Asp48, and noncovalent binding of cis-[V(IV)O(empp)(2)(H(2)O)], [V(IV)O(empp)(H(2)O)](+), [V(IV)O(empp)(H(2)O)(2)](+), and of an unusual trinuclear oxidovanadium(V) complex, [V(V)(3)O(6)(empp)(3)(H(2)O)], with accessible sites on the protein surface. The possibility of covalent and noncovalent binding with different strength and of interaction with various sites favor the formation of adducts with the multiple binding of vanadium moieties, allowing the transport in blood and cellular fluids of more than one metal-containing species with a possible amplification of the biological effects. Implications of Protein Interaction in the Speciation of Potential V(IV)O-Pyridinone Drugs.,Ferraro G, Paolillo M, Sciortino G, Pisanu F, Garribba E, Merlino A Inorg Chem. 2023 May 29;62(21):8407-8417. doi: 10.1021/acs.inorgchem.3c01041. , Epub 2023 May 17. PMID:37195003[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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