2xdc: Difference between revisions
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==Structure of linear gramicidin D obtained using Type I crystals grown in a lipid cubic phase.== | ==Structure of linear gramicidin D obtained using Type I crystals grown in a lipid cubic phase.== | ||
<StructureSection load='2xdc' size='340' side='right' | <StructureSection load='2xdc' size='340' side='right'caption='[[2xdc]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2xdc]] is a 6 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2xdc]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Brevibacillus_brevis Brevibacillus brevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XDC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XDC 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]] 1.7Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=15P:POLYETHYLENE+GLYCOL+(N=34)'>15P</scene>, <scene name='pdbligand=DLE:D-LEUCINE'>DLE</scene>, <scene name='pdbligand=DVA:D-VALINE'>DVA</scene>, <scene name='pdbligand=ETA:ETHANOLAMINE'>ETA</scene>, <scene name='pdbligand=FVA:N-FORMYL-L-VALINE'>FVA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PRD_000150:GRAMICIDIN+A'>PRD_000150</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=2xdc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xdc OCA], [https://pdbe.org/2xdc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xdc RCSB], [https://www.ebi.ac.uk/pdbsum/2xdc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xdc ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Brevibacillus brevis]] | [[Category: Brevibacillus brevis]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Aragao D]] | ||
[[Category: | [[Category: Caffrey M]] | ||
[[Category: | [[Category: Hoefer N]] | ||
Latest revision as of 08:35, 17 October 2024
Structure of linear gramicidin D obtained using Type I crystals grown in a lipid cubic phase.Structure of linear gramicidin D obtained using Type I crystals grown in a lipid cubic phase.
Structural highlights
Publication Abstract from PubMedStructure determination of membrane proteins by crystallographic means has been facilitated by crystallization in lipidic mesophases. It has been suggested, however, that this so-called in meso method, as originally implemented, would not apply to small protein targets having </=4 transmembrane crossings. In our study, the hypothesis that the inherent flexibility of the mesophase would enable crystallogenesis of small proteins was tested using a transmembrane pentadecapeptide, linear gramicidin, which produced structure-grade crystals. This result suggests that the in meso method should be considered as a viable means for high-resolution structure determination of integral membrane peptides, many of which are predicted to be coded for in the human genome. Crystallizing transmembrane peptides in lipidic mesophases.,Hofer N, Aragao D, Caffrey M Biophys J. 2010 Aug 4;99(3):L23-5. PMID:20682243[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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