3qe8: Difference between revisions

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==Crystal Structure Analysis of Lysozyme-bound fac-[Re(CO)3(H2O)(Im)]+==
The line below this paragraph, containing "STRUCTURE_3qe8", creates the "Structure Box" on the page.
<StructureSection load='3qe8' size='340' side='right'caption='[[3qe8]], [[Resolution|resolution]] 1.49&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.49&#8491;</td></tr>
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<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>
{{STRUCTURE_3qe8|  PDB=3qe8  |  SCENE=  }}
<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>
</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 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.


===Crystal Structure Analysis of Lysozyme-bound fac-[Re(CO)3(H2O)(Im)]+===
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<ref>PMID:22229733</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3qe8" style="background-color:#fffaf0;"></div>


==About this Structure==
==See Also==
[[3qe8]] is a 2 chain structure with sequence from [http://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].
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Lysozyme]]
[[Category: Large Structures]]
[[Category: Spingler, B.]]
[[Category: Spingler B]]
[[Category: Zobi, F.]]
[[Category: Zobi F]]
[[Category: Hydrolase]]
[[Category: Metallation]]
[[Category: Rhenium complex]]

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

3qe8 is a 2 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.49Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1]

Publication Abstract from PubMed

The 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 Also

References

  1. ↑ Maehashi K, Matano M, Irisawa T, Uchino M, Kashiwagi Y, Watanabe T. Molecular characterization of goose- and chicken-type lysozymes in emu (Dromaius novaehollandiae): evidence for extremely low lysozyme levels in emu egg white. Gene. 2012 Jan 15;492(1):244-9. doi: 10.1016/j.gene.2011.10.021. Epub 2011 Oct, 25. PMID:22044478 doi:10.1016/j.gene.2011.10.021
  2. ↑ Zobi F, Spingler B. Post-protein-binding reactivity and modifications of the fac-[Re(CO)3]+ core. Inorg Chem. 2012 Feb 6;51(3):1210-2. Epub 2012 Jan 9. PMID:22229733 doi:10.1021/ic2023314

3qe8, resolution 1.49Å

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