5v4h: Difference between revisions
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==Ruthenium(II)(cymene)(chlorido)2-lysozyme adduct formed when ruthenium(II)(cymene)(bromido)2 underwent ligand exchange, resulting in one binding site== | ==Ruthenium(II)(cymene)(chlorido)2-lysozyme adduct formed when ruthenium(II)(cymene)(bromido)2 underwent ligand exchange, resulting in one binding site== | ||
<StructureSection load='5v4h' size='340' side='right' caption='[[5v4h]], [[Resolution|resolution]] 1.22Å' scene=''> | <StructureSection load='5v4h' size='340' side='right'caption='[[5v4h]], [[Resolution|resolution]] 1.22Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5v4h]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5v4h]] 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=5V4H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5V4H FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.22Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=RU7:PARA-CYMENE+RUTHENIUM+CHLORIDE'>RU7</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=5v4h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v4h OCA], [https://pdbe.org/5v4h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5v4h RCSB], [https://www.ebi.ac.uk/pdbsum/5v4h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5v4h 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;"> | |||
== Publication Abstract from PubMed == | |||
Metalation of hen egg white lysozyme (HEWL) with organometallics was studied with physicochemical methods in solid state, solution and the gas phase. While metalation did not affect the crystal structure of HEWL significantly, protein destabilisation was detected in gas phase and solution. | |||
The metalation of hen egg white lysozyme impacts protein stability as shown by ion mobility mass spectrometry, differential scanning calorimetry, and X-ray crystallography.,Sullivan MP, Groessl M, Meier SM, Kingston RL, Goldstone DC, Hartinger CG Chem Commun (Camb). 2017 Apr 11;53(30):4246-4249. doi: 10.1039/c6cc10150j. PMID:28361137<ref>PMID:28361137</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5v4h" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Lysozyme 3D structures|Lysozyme 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 16: | Line 27: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Goldstone | [[Category: Goldstone DC]] | ||
[[Category: Hartinger | [[Category: Hartinger CG]] | ||
[[Category: Sullivan | [[Category: Sullivan MP]] | ||
Latest revision as of 16:41, 4 October 2023
Ruthenium(II)(cymene)(chlorido)2-lysozyme adduct formed when ruthenium(II)(cymene)(bromido)2 underwent ligand exchange, resulting in one binding siteRuthenium(II)(cymene)(chlorido)2-lysozyme adduct formed when ruthenium(II)(cymene)(bromido)2 underwent ligand exchange, resulting in one binding site
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 PubMedMetalation of hen egg white lysozyme (HEWL) with organometallics was studied with physicochemical methods in solid state, solution and the gas phase. While metalation did not affect the crystal structure of HEWL significantly, protein destabilisation was detected in gas phase and solution. The metalation of hen egg white lysozyme impacts protein stability as shown by ion mobility mass spectrometry, differential scanning calorimetry, and X-ray crystallography.,Sullivan MP, Groessl M, Meier SM, Kingston RL, Goldstone DC, Hartinger CG Chem Commun (Camb). 2017 Apr 11;53(30):4246-4249. doi: 10.1039/c6cc10150j. PMID:28361137[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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