3wpl: Difference between revisions

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New page: '''Unreleased structure''' The entry 3wpl is ON HOLD Authors: Mizutani, R., Saiga, R. Description: Soaking study of hen egg-white lysozyme crystal; derivative 2
 
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'''Unreleased structure'''


The entry 3wpl is ON HOLD
==SPATIOTEMPORAL DEVELOPMENT of SOAKED PROTEIN CRYSTAL; 2510 SEC==
<StructureSection load='3wpl' size='340' side='right'caption='[[3wpl]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3wpl]] 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=3WPL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WPL 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]] 2&#8491;</td></tr>
<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=3wpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wpl OCA], [https://pdbe.org/3wpl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wpl RCSB], [https://www.ebi.ac.uk/pdbsum/3wpl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wpl 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 ==
Crystal 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.


Authors: Mizutani, R., Saiga, R.
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<ref>PMID:25043871</ref>


Description: Soaking study of hen egg-white lysozyme crystal; derivative 2
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3wpl" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Large Structures]]
[[Category: Mizutani R]]
[[Category: Saiga R]]

Latest revision as of 16:21, 8 November 2023

SPATIOTEMPORAL DEVELOPMENT of SOAKED PROTEIN CRYSTAL; 2510 SECSPATIOTEMPORAL DEVELOPMENT of SOAKED PROTEIN CRYSTAL; 2510 SEC

Structural highlights

3wpl 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 2Å
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

Crystal 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 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. Mizutani R, Shimizu Y, Saiga R, Ueno G, Nakamura Y, Takeuchi A, Uesugi K, Suzuki Y. Spatiotemporal development of soaked protein crystal. Sci Rep. 2014 Jul 21;4:5731. doi: 10.1038/srep05731. PMID:25043871 doi:http://dx.doi.org/10.1038/srep05731

3wpl, resolution 2.00Å

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