6f9y: Difference between revisions
New page: '''Unreleased structure''' The entry 6f9y is ON HOLD Authors: Camara-Artigas, A. Description: Lysozyme crystallized in presence of 10 mM lithium sulphate at pH 4.5 [[Category: Unreleas... |
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The | ==Lysozyme crystallized in presence of 10 mM lithium sulphate at pH 4.5== | ||
<StructureSection load='6f9y' size='340' side='right'caption='[[6f9y]], [[Resolution|resolution]] 1.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6f9y]] 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=6F9Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6F9Y 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]] 1.2Å</td></tr> | |||
<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=SO4:SULFATE+ION'>SO4</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=6f9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f9y OCA], [https://pdbe.org/6f9y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6f9y RCSB], [https://www.ebi.ac.uk/pdbsum/6f9y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6f9y 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 structure of orthorhombic lysozyme has been obtained at 298 K and pH 4.5 using sodium chloride as the precipitant and in the presence of sodium phosphate at a concentration as low as 5 mM. Crystals belonging to space group P212121 (unit-cell parameters a = 30, b = 56, c = 73 A, alpha = beta = gamma = 90.00 degrees ) diffracted to a resolution higher than 1 A, and the high quality of these crystals permitted the identification of a phosphate ion bound to Arg14 and His15. The binding of this ion produces long-range conformational changes affecting the loop containing Ser60-Asn74. The negatively charged phosphate ion shields the electrostatic repulsion of the positively charged arginine and histidine residues, resulting in higher stability of the phosphate-bound lysozyme. Additionally, a low-humidity orthorhombic variant was obtained at pH 4.5, and comparison with those previously obtained at pH 6.5 and 9.5 shows a 1.5 A displacement of the fifth alpha-helix towards the active-site cavity, which might be relevant to protein function. Since lysozyme is broadly used as a model protein in studies related to protein crystallization and amyloid formation, these results indicate that the interaction of some anions must be considered when analysing experiments performed at acidic pH values. | |||
Orthorhombic lysozyme crystallization at acidic pH values driven by phosphate binding.,Plaza-Garrido M, Salinas-Garcia MC, Camara-Artigas A Acta Crystallogr D Struct Biol. 2018 May 1;74(Pt 5):480-489. doi:, 10.1107/S205979831800517X. Epub 2018 Apr 27. PMID:29717719<ref>PMID:29717719</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Camara-Artigas | <div class="pdbe-citations 6f9y" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Lysozyme 3D structures|Lysozyme 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Gallus gallus]] | |||
[[Category: Large Structures]] | |||
[[Category: Camara-Artigas A]] | |||
Latest revision as of 12:00, 9 October 2024
Lysozyme crystallized in presence of 10 mM lithium sulphate at pH 4.5Lysozyme crystallized in presence of 10 mM lithium sulphate at pH 4.5
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 PubMedThe structure of orthorhombic lysozyme has been obtained at 298 K and pH 4.5 using sodium chloride as the precipitant and in the presence of sodium phosphate at a concentration as low as 5 mM. Crystals belonging to space group P212121 (unit-cell parameters a = 30, b = 56, c = 73 A, alpha = beta = gamma = 90.00 degrees ) diffracted to a resolution higher than 1 A, and the high quality of these crystals permitted the identification of a phosphate ion bound to Arg14 and His15. The binding of this ion produces long-range conformational changes affecting the loop containing Ser60-Asn74. The negatively charged phosphate ion shields the electrostatic repulsion of the positively charged arginine and histidine residues, resulting in higher stability of the phosphate-bound lysozyme. Additionally, a low-humidity orthorhombic variant was obtained at pH 4.5, and comparison with those previously obtained at pH 6.5 and 9.5 shows a 1.5 A displacement of the fifth alpha-helix towards the active-site cavity, which might be relevant to protein function. Since lysozyme is broadly used as a model protein in studies related to protein crystallization and amyloid formation, these results indicate that the interaction of some anions must be considered when analysing experiments performed at acidic pH values. Orthorhombic lysozyme crystallization at acidic pH values driven by phosphate binding.,Plaza-Garrido M, Salinas-Garcia MC, Camara-Artigas A Acta Crystallogr D Struct Biol. 2018 May 1;74(Pt 5):480-489. doi:, 10.1107/S205979831800517X. Epub 2018 Apr 27. PMID:29717719[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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