3ru5: Difference between revisions

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'''Unreleased structure'''


The entry 3ru5 is ON HOLD
==Silver Metallated Hen Egg White Lysozyme at 1.35 A==
<StructureSection load='3ru5' size='340' side='right'caption='[[3ru5]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3ru5]] 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=3RU5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RU5 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]] 1.35&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AG:SILVER+ION'>AG</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</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=3ru5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ru5 OCA], [https://pdbe.org/3ru5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ru5 RCSB], [https://www.ebi.ac.uk/pdbsum/3ru5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ru5 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 X-ray crystal structure, NMR binding studies, and enzyme activity of silver(i) metallated hen egg white lysozyme are presented. Primary bonding of silver is observed through His15 with secondary bonding interactions coming from nearby Arg14 and Asp87. A covalently bound nitrate completes a four coordinate binding pocket.


Authors: Leeper, T.C., Panzner, M.J., Bilinovich, S.M.
Silver metallation of hen egg white lysozyme: X-ray crystal structure and NMR studies.,Panzner MJ, Bilinovich SM, Youngs WJ, Leeper TC Chem Commun (Camb). 2011 Dec 14;47(46):12479-81. Epub 2011 Oct 31. PMID:22042312<ref>PMID:22042312</ref>


Description: Silver Metallated Hen Egg White Lysozyme at 1.35 A
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ru5" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Large Structures]]
[[Category: Bilinovich SM]]
[[Category: Leeper TC]]
[[Category: Panzner MJ]]

Latest revision as of 09:44, 27 November 2024

Silver Metallated Hen Egg White Lysozyme at 1.35 ASilver Metallated Hen Egg White Lysozyme at 1.35 A

Structural highlights

3ru5 is a 1 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 1.35Å
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 X-ray crystal structure, NMR binding studies, and enzyme activity of silver(i) metallated hen egg white lysozyme are presented. Primary bonding of silver is observed through His15 with secondary bonding interactions coming from nearby Arg14 and Asp87. A covalently bound nitrate completes a four coordinate binding pocket.

Silver metallation of hen egg white lysozyme: X-ray crystal structure and NMR studies.,Panzner MJ, Bilinovich SM, Youngs WJ, Leeper TC Chem Commun (Camb). 2011 Dec 14;47(46):12479-81. Epub 2011 Oct 31. PMID:22042312[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. ↑ Panzner MJ, Bilinovich SM, Youngs WJ, Leeper TC. Silver metallation of hen egg white lysozyme: X-ray crystal structure and NMR studies. Chem Commun (Camb). 2011 Dec 14;47(46):12479-81. Epub 2011 Oct 31. PMID:22042312 doi:10.1039/c1cc15908a

3ru5, resolution 1.35Å

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