9bic
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==N-Me-D-Leu2,D-Thr5-clovibactin== | |
| + | <StructureSection load='9bic' size='340' side='right'caption='[[9bic]], [[Resolution|resolution]] 2.05Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9bic]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Eleftheria Eleftheria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9BIC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9BIC 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]] 2.05Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=DLY:D-LYSINE'>DLY</scene>, <scene name='pdbligand=DTH:D-THREONINE'>DTH</scene>, <scene name='pdbligand=MLU:N-METHYL-D-LEUCINE'>MLU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=9bic FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9bic OCA], [https://pdbe.org/9bic PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9bic RCSB], [https://www.ebi.ac.uk/pdbsum/9bic PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9bic ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Our laboratory reported the chemical synthesis and stereochemical assignment of the recently discovered peptide antibiotic clovibactin. The current paper reports an improved, gram-scale synthesis of the amino acid building block Fmoc-(2R,3R)-3-hydroxyasparagine-OH that enables structure-activity relationship studies of clovibactin. An alanine scan reveals that residues Phe(1), d-Leu(2), Ser(4), Leu(7), and Leu(8) are important for antibiotic activity. The side-chain amide group of the rare d-Hyn(5) residue is not essential to activity and can be replaced with a methyl group with a moderate loss of activity. An acyclic clovibactin analogue reveals that the macrolactone ring is essential to antibiotic activity. The enantiomer of clovibactin is active, albeit somewhat less so than clovibactin. A conformationally constrained clovibactin analogue retains moderate antibiotic activity, while a backbone N-methylated analogue is almost completely inactive. X-ray crystallography of these two analogues reveals that the macrolactone ring adopts a crown-like conformation that binds anions. | ||
| - | + | Structure-Activity Relationship Studies of the Peptide Antibiotic Clovibactin.,Brunicardi JEH, Griffin JH, Ferracane MJ, Kreutzer AG, Small J, Mendoza AT, Ziller JW, Nowick JS J Org Chem. 2024 Sep 6;89(17):12479-12484. doi: 10.1021/acs.joc.4c01414. Epub , 2024 Aug 23. PMID:39178334<ref>PMID:39178334</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 9bic" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Eleftheria]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Griffin JG]] | ||
| + | [[Category: Kreutzer AG]] | ||
| + | [[Category: Nowick JS]] | ||
Current revision
N-Me-D-Leu2,D-Thr5-clovibactin
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