View source for 7nef


==Fucosylated linear peptide Fln65 bound to the fucose binding lectin LecB PA-IIL from Pseudomonas aeruginosa at 1.5 Angstrom resolution==
<StructureSection load='7nef' size='340' side='right'caption='[[7nef]], [[Resolution|resolution]] 1.51&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7nef]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NEF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NEF 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]] 1.51&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=ZDC:3,7-ANHYDRO-2,8-DIDEOXY-L-GLYCERO-D-GLUCO-OCTONIC+ACID'>ZDC</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=7nef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nef OCA], [https://pdbe.org/7nef PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nef RCSB], [https://www.ebi.ac.uk/pdbsum/7nef PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nef ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9HYN5_PSEAE Q9HYN5_PSEAE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The peptide alpha-helix is right-handed when containing amino acids with l-chirality, and left-handed with d-chirality, however mixed chirality peptides generally do not form alpha-helices unless a helix inducer such as the non-natural residue amino-isobutyric acid is used. Herein we report the first X-ray crystal structures of mixed chirality alpha-helices in short peptides comprising only natural residues as the example of a stapled bicyclic and a linear membrane disruptive amphiphilic antimicrobial peptide (AMP) containing seven l- and four d-residues, as complexes of fucosylated analogs with the bacterial lectin LecB. The mixed chirality alpha-helices are superimposable onto the homochiral alpha-helices and form under similar conditions as shown by CD spectra and MD simulations but non-hemolytic and resistant to proteolysis. The observation of a mixed chirality alpha-helix with only natural residues in the protein environment of LecB suggests a vast unexplored territory of alpha-helical mixed chirality sequences and their possible use for optimizing bioactive alpha-helical peptides.

A mixed chirality alpha-helix in a stapled bicyclic and a linear antimicrobial peptide revealed by X-ray crystallography.,Baeriswyl S, Personne H, Di Bonaventura I, Kohler T, van Delden C, Stocker A, Javor S, Reymond JL RSC Chem Biol. 2021 Aug 20;2(6):1608-1617. doi: 10.1039/d1cb00124h. eCollection, 2021 Dec 2. PMID:34977576<ref>PMID:34977576</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7nef" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Synthetic construct]]
[[Category: Baeriswyl S]]
[[Category: Personne H]]
[[Category: Reymond J-L]]
[[Category: Stocker A]]