3qe8: Difference between revisions

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[[Image:3qe8.png|left|200px]]
==Crystal Structure Analysis of Lysozyme-bound fac-[Re(CO)3(H2O)(Im)]+==
<StructureSection load='3qe8' size='340' side='right' caption='[[3qe8]], [[Resolution|resolution]] 1.49&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3qng|3qng]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qe8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qe8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qe8 RCSB], [http://www.ebi.ac.uk/pdbsum/3qe8 PDBsum]</span></td></tr>
</table>
<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.


{{STRUCTURE_3qe8|  PDB=3qe8  |  SCENE=  }}
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>


===Crystal Structure Analysis of Lysozyme-bound fac-[Re(CO)3(H2O)(Im)]+===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_22229733}}
 
==About this Structure==
[[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].


==See Also==
==See Also==
*[[Hen Egg-White (HEW) Lysozyme|Hen Egg-White (HEW) Lysozyme]]
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:022229733</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Lysozyme]]
[[Category: Lysozyme]]
[[Category: Spingler, B.]]
[[Category: Spingler, B]]
[[Category: Zobi, F.]]
[[Category: Zobi, F]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Metallation]]
[[Category: Metallation]]
[[Category: Rhenium complex]]
[[Category: Rhenium complex]]

Revision as of 15:33, 9 December 2014

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.
Ligands:, ,
Activity:Lysozyme, with EC number 3.2.1.17
Resources:FirstGlance, OCA, RCSB, PDBsum

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. 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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