7q0x: Difference between revisions

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<StructureSection load='7q0x' size='340' side='right'caption='[[7q0x]], [[Resolution|resolution]] 1.09&Aring;' scene=''>
<StructureSection load='7q0x' size='340' side='right'caption='[[7q0x]], [[Resolution|resolution]] 1.09&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7q0x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Q0X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Q0X FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Q0X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Q0X 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]] 1.09&#8491;</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]] 1.09&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6PC:PYRIDINE-2-CARBOXYLIC+ACID'>6PC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=V:VANADIUM+ION'>V</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6PC:PYRIDINE-2-CARBOXYLIC+ACID'>6PC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=7q0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7q0x OCA], [https://pdbe.org/7q0x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7q0x RCSB], [https://www.ebi.ac.uk/pdbsum/7q0x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7q0x 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=7q0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7q0x OCA], [https://pdbe.org/7q0x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7q0x RCSB], [https://www.ebi.ac.uk/pdbsum/7q0x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7q0x ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TRY1_BOVIN TRY1_BOVIN]
<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>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7q0x" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Trypsin 3D structures|Trypsin 3D structures]]
*[[Trypsin 3D structures|Trypsin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Correia I]]
[[Category: Correia I]]

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