6agn: Difference between revisions
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==Structure of HEWL co-crystallised with Cinnamaldehyde== | |||
<StructureSection load='6agn' size='340' side='right'caption='[[6agn]], [[Resolution|resolution]] 1.08Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6agn]] 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=6AGN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AGN 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]] 1.08Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9Y3:(2Z)-3-phenylprop-2-enal'>9Y3</scene>, <scene name='pdbligand=9Y6:(~{E})-3-phenylprop-2-enal'>9Y6</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=6agn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6agn OCA], [https://pdbe.org/6agn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6agn RCSB], [https://www.ebi.ac.uk/pdbsum/6agn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6agn 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 == | |||
Release of water is the main force which drives proteins towards crystallisation (giving rise to protein crystals for crystallography) and aggregation (main cause of neurodegenerative diseases), and as such it is possible to make changes in the crystallisation/aggregation process by using compounds which are able to reduce the amount of water molecules around proteins. Cinnamaldehyde and Phenyl ethyl alcohol are the active constituents of cinnamon and rose flower, respectively. Traditional Iranian Medicine (TIM) suggests the use of cinnamon and rose flower for the reduction of excess coldness and wetness from the brain of patients suffering from Dementia. Using crystallisation as a model system and X-ray crystallography, we tested whether Cinnamaldehyde or Phenyl ethyl alcohol can mimic the role of precipitants resulting in the formation of crystals of HEWL (as a model protein) by releasing water from the surrounding protein environment. Results have revealed that both Cinnamaldehyde and Phenyl ethyl alcohol, in particular, were capable to adequately act as 'precipitants' but in the presence of NaCl (as a salt), resulting in better crystals of HEWL by changing the amount of charge and/or making water molecules unavailable in the symmetry related position, in line with the role suggested for these compounds by TIM. | |||
The role of Cinnamaldehyde and Phenyl ethyl alcohol as two types of precipitants affecting protein hydration levels.,Seraj Z, Seyedarabi A Int J Biol Macromol. 2019 Dec 27;146:705-715. doi:, 10.1016/j.ijbiomac.2019.12.204. PMID:31887389<ref>PMID:31887389</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6agn" style="background-color:#fffaf0;"></div> | ||
[[Category: Seraj | |||
==See Also== | |||
*[[Lysozyme 3D structures|Lysozyme 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Gallus gallus]] | |||
[[Category: Large Structures]] | |||
[[Category: Seraj Z]] | |||
[[Category: Seyedarabi A]] | |||
Latest revision as of 15:25, 6 November 2024
Structure of HEWL co-crystallised with CinnamaldehydeStructure of HEWL co-crystallised with Cinnamaldehyde
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 PubMedRelease of water is the main force which drives proteins towards crystallisation (giving rise to protein crystals for crystallography) and aggregation (main cause of neurodegenerative diseases), and as such it is possible to make changes in the crystallisation/aggregation process by using compounds which are able to reduce the amount of water molecules around proteins. Cinnamaldehyde and Phenyl ethyl alcohol are the active constituents of cinnamon and rose flower, respectively. Traditional Iranian Medicine (TIM) suggests the use of cinnamon and rose flower for the reduction of excess coldness and wetness from the brain of patients suffering from Dementia. Using crystallisation as a model system and X-ray crystallography, we tested whether Cinnamaldehyde or Phenyl ethyl alcohol can mimic the role of precipitants resulting in the formation of crystals of HEWL (as a model protein) by releasing water from the surrounding protein environment. Results have revealed that both Cinnamaldehyde and Phenyl ethyl alcohol, in particular, were capable to adequately act as 'precipitants' but in the presence of NaCl (as a salt), resulting in better crystals of HEWL by changing the amount of charge and/or making water molecules unavailable in the symmetry related position, in line with the role suggested for these compounds by TIM. The role of Cinnamaldehyde and Phenyl ethyl alcohol as two types of precipitants affecting protein hydration levels.,Seraj Z, Seyedarabi A Int J Biol Macromol. 2019 Dec 27;146:705-715. doi:, 10.1016/j.ijbiomac.2019.12.204. PMID:31887389[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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