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6pq0

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'''Unreleased structure'''
 
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The entry 6pq0 is ON HOLD until Paper Publication
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==LCP-embedded Proteinase K treated with MPD==
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<StructureSection load='6pq0' size='340' side='right'caption='[[6pq0]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6pq0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Parengyodontium_album Parengyodontium album]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PQ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PQ0 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron crystallography, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6pq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pq0 OCA], [https://pdbe.org/6pq0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pq0 RCSB], [https://www.ebi.ac.uk/pdbsum/6pq0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pq0 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PRTK_PARAQ PRTK_PARAQ] Hydrolyzes keratin at aromatic and hydrophobic residues.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The lipidic cubic phase (LCP) technique has proved to facilitate the growth of high-quality crystals that are otherwise difficult to grow by other methods. However, the crystal size optimization process could be time and resource consuming, if it ever happens. Therefore, improved techniques for structure determination using these small crystals is an important strategy in diffraction technology development. Microcrystal electron diffraction (MicroED) is a technique that uses a cryo-transmission electron microscopy to collect electron diffraction data and determine high-resolution structures from very thin micro- and nanocrystals. In this work, we have used modified LCP and MicroED protocols to analyze crystals embedded in LCP converted by 2-methyl-2,4-pentanediol or lipase, including Proteinase K crystals grown in solution, cholesterol crystals, and human adenosine A2A receptor crystals grown in LCP. These results set the stage for the use of MicroED to analyze microcrystalline samples grown in LCP, especially for those highly challenging membrane protein targets.
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Authors:
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Structure Determination from Lipidic Cubic Phase Embedded Microcrystals by MicroED.,Zhu L, Bu G, Jing L, Shi D, Lee MY, Gonen T, Liu W, Nannenga BL Structure. 2020 Jul 28. pii: S0969-2126(20)30239-2. doi:, 10.1016/j.str.2020.07.006. PMID:32735770<ref>PMID:32735770</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6pq0" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Proteinase 3D structures|Proteinase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Parengyodontium album]]
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[[Category: Bu G]]
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[[Category: Gonen T]]
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[[Category: Jing L]]
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[[Category: Liu W]]
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[[Category: Nannenga BL]]
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[[Category: Shi D]]
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[[Category: Zhu L]]

Current revision

LCP-embedded Proteinase K treated with MPD

PDB ID 6pq0

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