6tvl: Difference between revisions
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==Hen Egg White Lysozyme in complex with a "half sandwich"-type Ru(II) coordination compound== | |||
<StructureSection load='6tvl' size='340' side='right'caption='[[6tvl]], [[Resolution|resolution]] 1.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6tvl]] 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=6TVL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TVL 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]] 1.395Å</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>, <scene name='pdbligand=NYN:chlorido(1,2-diaminoethane-k2N,N)(1,4,7-trithiacyclononane-k3S,S,S)ruthenium(II)+trifluoromethanesulfonate'>NYN</scene>, <scene name='pdbligand=TFS:TRIFLUOROMETHANESULFONIC+ACID'>TFS</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=6tvl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tvl OCA], [https://pdbe.org/6tvl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tvl RCSB], [https://www.ebi.ac.uk/pdbsum/6tvl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tvl 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 == | |||
The high-resolution X-ray crystal structures of the adducts formed between the "half sandwich"-type Ru(II) coordination compound [Ru(II)(1,4,7-trithiacyclononane)(ethane-1,2-diamine)Cl](+) and two proteins, namely hen egg-white lysozyme and proteinase K, are presented. The structures unveil that upon reaction with both enzymes the Ru(II) compound is coordinated by solvent-exposed aspartate residues after releasing the chloride ligand (Asp101 in lysozyme, Asp200 and Asp260 in proteinase K), while retaining the two chelating ligands. The adduct with Asp101 residue at the catalytic cleft of lysozyme is accompanied by residue-specific conformational changes to accommodate the Ru(II) fragment, whereas the complexes bound at the two calcium-binding sites of proteinase K revealed minimal structural perturbation of the enzyme. To the best of our knowledge, proteinase K is used here for the first time as a model system of protein metalation and these are the first X-ray crystal structures of protein adducts of a Ru(II) coordination compound that maintains its coordination sphere almost intact upon binding. Our data demonstrate the role of ligands in stabilizing the protein adducts via hydrophobic/aromatic or hydrogen-bonding interactions, as well as their underlying role in the selection of specific sites on the electrostatic potential surface of the enzymes. | |||
High-resolution crystal structures of a "half sandwich"-type Ru(II) coordination compound bound to hen egg-white lysozyme and proteinase K.,Chiniadis L, Bratsos I, Bethanis K, Karpusas M, Giastas P, Papakyriakou A J Biol Inorg Chem. 2020 Apr 8. pii: 10.1007/s00775-020-01786-z. doi:, 10.1007/s00775-020-01786-z. PMID:32266561<ref>PMID:32266561</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6tvl" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Lysozyme 3D structures|Lysozyme 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Gallus gallus]] | |||
[[Category: Large Structures]] | |||
[[Category: Bratsos I]] | |||
[[Category: Chiniadis L]] | |||
[[Category: Giastas P]] | |||
[[Category: Papakyriakou A]] | |||
Latest revision as of 16:10, 24 January 2024
Hen Egg White Lysozyme in complex with a "half sandwich"-type Ru(II) coordination compoundHen Egg White Lysozyme in complex with a "half sandwich"-type Ru(II) coordination compound
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 PubMedThe high-resolution X-ray crystal structures of the adducts formed between the "half sandwich"-type Ru(II) coordination compound [Ru(II)(1,4,7-trithiacyclononane)(ethane-1,2-diamine)Cl](+) and two proteins, namely hen egg-white lysozyme and proteinase K, are presented. The structures unveil that upon reaction with both enzymes the Ru(II) compound is coordinated by solvent-exposed aspartate residues after releasing the chloride ligand (Asp101 in lysozyme, Asp200 and Asp260 in proteinase K), while retaining the two chelating ligands. The adduct with Asp101 residue at the catalytic cleft of lysozyme is accompanied by residue-specific conformational changes to accommodate the Ru(II) fragment, whereas the complexes bound at the two calcium-binding sites of proteinase K revealed minimal structural perturbation of the enzyme. To the best of our knowledge, proteinase K is used here for the first time as a model system of protein metalation and these are the first X-ray crystal structures of protein adducts of a Ru(II) coordination compound that maintains its coordination sphere almost intact upon binding. Our data demonstrate the role of ligands in stabilizing the protein adducts via hydrophobic/aromatic or hydrogen-bonding interactions, as well as their underlying role in the selection of specific sites on the electrostatic potential surface of the enzymes. High-resolution crystal structures of a "half sandwich"-type Ru(II) coordination compound bound to hen egg-white lysozyme and proteinase K.,Chiniadis L, Bratsos I, Bethanis K, Karpusas M, Giastas P, Papakyriakou A J Biol Inorg Chem. 2020 Apr 8. pii: 10.1007/s00775-020-01786-z. doi:, 10.1007/s00775-020-01786-z. PMID:32266561[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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