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<StructureSection load='7q0v' size='340' side='right'caption='[[7q0v]], [[Resolution|resolution]] 1.12&Aring;' scene=''>
<StructureSection load='7q0v' size='340' side='right'caption='[[7q0v]], [[Resolution|resolution]] 1.12&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7q0v]] 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=7Q0V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Q0V FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Q0V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Q0V 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=O:OXYGEN+ATOM'>O</scene>, <scene name='pdbligand=PHN:1,10-PHENANTHROLINE'>PHN</scene>, <scene name='pdbligand=V:VANADIUM+ION'>V</scene></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]] 1.12&#8491;</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=O:OXYGEN+ATOM'>O</scene>, <scene name='pdbligand=PHN:1,10-PHENANTHROLINE'>PHN</scene>, <scene name='pdbligand=V:VANADIUM+ION'>V</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=7q0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7q0v OCA], [https://pdbe.org/7q0v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7q0v RCSB], [https://www.ebi.ac.uk/pdbsum/7q0v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7q0v 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=7q0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7q0v OCA], [https://pdbe.org/7q0v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7q0v RCSB], [https://www.ebi.ac.uk/pdbsum/7q0v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7q0v 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 ==
Vanadium compounds have frequently been proposed as therapeutics, but their application has been hampered by the lack of information on the different V-containing species that may form and how these interact with blood and cell proteins, and with enzymes. Herein, we report several resolved crystal structures of lysozyme with bound V(IV) O(2+) and V(IV) OL(2+) , where L=2,2'-bipyridine or 1,10-phenanthroline (phen), and of trypsin with V(IV) O(picolinato)2 and V(V) O2 (phen)(+) moieties. Computational studies complete the refinement and shed light on the relevant role of hydrophobic interactions, hydrogen bonds, and microsolvation in stabilizating the structure. Noteworthy is that the trypsin-V(V) O2 (phen) and trypsin-V(IV) O(OH)(phen) adducts correspond to similar energies, thus suggesting a possible interconversion under physiological/biological conditions. The obtained data support the relevance of hydrolysis of V(IV) and V(V) complexes in the several types of binding established with proteins and the formation of different adducts that might contribute to their pharmacological action, and significantly widen our knowledge of vanadium-protein interactions.


Binding of V(IV) O(2+) , V(IV) OL, V(IV) OL2 and V(V) O2 L Moieties to Proteins: X-ray/Theoretical Characterization and Biological Implications.,Santos MFA, Sciortino G, Correia I, Fernandes ACP, Santos-Silva T, Pisanu F, Garribba E, Costa Pessoa J Chemistry. 2022 Apr 29:e202200105. doi: 10.1002/chem.202200105. PMID:35486702<ref>PMID:35486702</ref>
==See Also==
 
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7q0v" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Correia I]]
[[Category: Correia I]]

Latest revision as of 12:05, 17 October 2024

Lysozyme soaked with V(IV)OSO4 and phenLysozyme soaked with V(IV)OSO4 and phen

Structural highlights

Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.12Å
Ligands:, , , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

See Also

7q0v, resolution 1.12Å

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