3wu9: Difference between revisions
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==Spatiotemporal development of soaked protein crystal; derivative 1580 sec== | ==Spatiotemporal development of soaked protein crystal; derivative 1580 sec== | ||
<StructureSection load='3wu9' size='340' side='right' caption='[[3wu9]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='3wu9' size='340' side='right'caption='[[3wu9]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3wu9]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3wu9]] 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=3WU9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WU9 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]] 2Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PT4:PLATINUM+(IV)+ION'>PT4</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=3wu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wu9 OCA], [https://pdbe.org/3wu9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wu9 RCSB], [https://www.ebi.ac.uk/pdbsum/3wu9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wu9 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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 20: | Line 19: | ||
</div> | </div> | ||
<div class="pdbe-citations 3wu9" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3wu9" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Lysozyme 3D structures|Lysozyme 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Mizutani | [[Category: Mizutani R]] | ||
[[Category: Saiga | [[Category: Saiga R]] | ||
Latest revision as of 16:29, 8 November 2023
Spatiotemporal development of soaked protein crystal; derivative 1580 secSpatiotemporal development of soaked protein crystal; derivative 1580 sec
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 PubMedCrystal soaking is widely performed in biological crystallography. This paper reports time-resolved X-ray crystallographic and microtomographic analyses of tetragonal crystals of chicken egg-white lysozyme soaked in mother liquor containing potassium hexachloroplatinate. The microtomographic analysis showed that X-ray attenuation spread from the superficial layer of the crystal and then to the crystal core. The crystallographic analyses indicated that platinum sites can be classified into two groups from the temporal development of the electron densities. A soaking process consisting of binding-rate-driven and equilibrium-driven layers is proposed to describe these results. This study suggests that the composition of chemical and structural species resulting from the soaking process varies depending on the position in the crystal. Spatiotemporal development of soaked protein crystal.,Mizutani R, Shimizu Y, Saiga R, Ueno G, Nakamura Y, Takeuchi A, Uesugi K, Suzuki Y Sci Rep. 2014 Jul 21;4:5731. doi: 10.1038/srep05731. PMID:25043871[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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