3qe8: Difference between revisions
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==Crystal Structure Analysis of Lysozyme-bound fac-[Re(CO)3(H2O)(Im)]+== | ==Crystal Structure Analysis of Lysozyme-bound fac-[Re(CO)3(H2O)(Im)]+== | ||
<StructureSection load='3qe8' size='340' side='right' caption='[[3qe8]], [[Resolution|resolution]] 1.49Å' scene=''> | <StructureSection load='3qe8' size='340' side='right'caption='[[3qe8]], [[Resolution|resolution]] 1.49Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3qe8]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3qe8]] is a 2 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=3QE8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QE8 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=REI:TRICARBONYL+(AQUA)+(IMIDAZOLE)+RHENIUM(I)'>REI</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.49Å</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=REI:TRICARBONYL+(AQUA)+(IMIDAZOLE)+RHENIUM(I)'>REI</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=3qe8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qe8 OCA], [https://pdbe.org/3qe8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qe8 RCSB], [https://www.ebi.ac.uk/pdbsum/3qe8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qe8 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == 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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 18: | Line 18: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3qe8" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
| Line 26: | Line 27: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Spingler | [[Category: Spingler B]] | ||
[[Category: Zobi | [[Category: Zobi F]] | ||
Latest revision as of 20:12, 1 November 2023
Crystal Structure Analysis of Lysozyme-bound fac-[Re(CO)3(H2O)(Im)]+Crystal Structure Analysis of Lysozyme-bound fac-[Re(CO)3(H2O)(Im)]+
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 reactivity of the [Re(CO)(3)(H(2)O)(2)](+) complex coordinated to the His15 residue of HEW lysozyme is described. In the fully metalated protein (Lys-1), the Re ion retains its reactivity only toward selected ligands, while others induce a ligand-mediated demetalation of the enzyme. It is further shown that some of the complexes that may be "engineered" on the lysozyme do not react with the free protein even if present in solution in excess. The formation of stable metal adducts starting from Lys-1 was confirmed by X-ray crystallography. Post-protein-binding reactivity and modifications of the fac-[Re(CO)3]+ core.,Zobi F, Spingler B Inorg Chem. 2012 Feb 6;51(3):1210-2. Epub 2012 Jan 9. PMID:22229733[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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