3e7r: Difference between revisions
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<StructureSection load='3e7r' size='340' side='right'caption='[[3e7r]], [[Resolution|resolution]] 1.00Å' scene=''> | <StructureSection load='3e7r' size='340' side='right'caption='[[3e7r]], [[Resolution|resolution]] 1.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3e7r]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E7R OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[3e7r]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E7R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E7R FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3e7u|3e7u]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3e7u|3e7u]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3e7r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e7r OCA], [https://pdbe.org/3e7r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e7r RCSB], [https://www.ebi.ac.uk/pdbsum/3e7r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e7r ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Revision as of 08:33, 15 June 2022
X-ray Crystal Structure of Racemic PlectasinX-ray Crystal Structure of Racemic Plectasin
Structural highlights
Publication Abstract from PubMedWe describe the use of racemic crystallography to determine the X-ray structure of the natural product plectasin, a potent antimicrobial protein recently isolated from fungus. The protein enantiomers L-plectasin and D-plectasin were prepared by total chemical synthesis; interestingly, L-plectasin showed the expected antimicrobial activity, while D-plectasin was devoid of such activity. The mirror image proteins were then used for racemic crystallization. Synchrotron X-ray diffraction data were collected to atomic resolution from a racemic plectasin crystal; the racemate crystallized in the achiral centrosymmetric space group P1 with one L-plectasin molecule and one D-plectasin molecule forming the unit cell. Dimer-like intermolecular interactions between the protein enantiomers were observed, which may account for the observed extremely low solvent content (13%-15%) and more highly ordered nature of the racemic crystals. The structure of the plectasin molecule was well defined for all 40 amino acids and was generally similar to the previously determined NMR structure, suggesting minimal impact of the crystal packing on the plectasin conformation. Racemic crystallography of synthetic protein enantiomers used to determine the X-ray structure of plectasin by direct methods.,Mandal K, Pentelute BL, Tereshko V, Thammavongsa V, Schneewind O, Kossiakoff AA, Kent SB Protein Sci. 2009 Jun;18(6):1146-54. PMID:19472324[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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