6w8e

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Current revision (13:15, 6 November 2024) (edit) (undo)
 
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<StructureSection load='6w8e' size='340' side='right'caption='[[6w8e]], [[Resolution|resolution]] 2.68&Aring;' scene=''>
<StructureSection load='6w8e' size='340' side='right'caption='[[6w8e]], [[Resolution|resolution]] 2.68&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6w8e]] 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=6W8E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6W8E FirstGlance]. <br>
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6W8E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6W8E 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]] 2.68&#8491;</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.68&#8491;</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></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></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=6w8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6w8e OCA], [https://pdbe.org/6w8e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6w8e RCSB], [https://www.ebi.ac.uk/pdbsum/6w8e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6w8e ProSAT]</span></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=6w8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6w8e OCA], [https://pdbe.org/6w8e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6w8e RCSB], [https://www.ebi.ac.uk/pdbsum/6w8e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6w8e ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
 
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[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>
 
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Catalyzing life-sustaining reactions, proteins are composed by 20 different amino acids that fold into a compact yet flexible three-dimensional architecture, which dictates what their function(s) might be. Determining the spatial arrangement of the atoms, the protein's 3D structure, enables key advances in fundamental and applied research. Protein crystallization is a powerful technique to achieve this. Unlike Earth's crystallization experiments, biomolecular crystallization in space in the absence of gravitational force is actively sought to improve crystal growth techniques. However, the effects of changing gravitational vectors on a protein solution reaching supersaturation remain largely unknown. Here, we have developed a low-cost crystallization cell within a CubeSat payload module to exploit the unique experimental conditions set aboard a sounding rocket. We designed a biaxial gimbal to house the crystallization experiments and take measurements on the protein solution in-flight with a spectrophotometry system. After flight, we used X-ray diffraction analysis to determine that flown protein has a structural rearrangement marked by loss of the protein's water and sodium in a manner that differs from crystals grown on the ground. We finally show that our gimbal payload module design is a portable experimental setup to take laboratory research investigations into exploratory space flights.
 
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Protein structural changes on a CubeSat under rocket acceleration profile.,Luna A, Meisel J, Hsu K, Russi S, Fernandez D NPJ Microgravity. 2020 Apr 23;6:12. doi: 10.1038/s41526-020-0102-3. eCollection, 2020. PMID:32352028<ref>PMID:32352028</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 6w8e" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Gallus gallus]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Fernandez D]]
[[Category: Fernandez D]]
[[Category: Russi S]]
[[Category: Russi S]]

Current revision

Crystal Structure Analysis of Space-grown Lysozyme

PDB ID 6w8e

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