View source for 9bni


==X-ray crystal structure of Cu-TZ4H-H3AH10D tryptophan zipper metallo-beta-sheet peptide==
<StructureSection load='9bni' size='340' side='right'caption='[[9bni]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9bni]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9BNI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9BNI 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]] 1.2&#8491;</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=9bni FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9bni OCA], [https://pdbe.org/9bni PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9bni RCSB], [https://www.ebi.ac.uk/pdbsum/9bni PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9bni ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Metal binding to beta-sheets occurs in many metalloproteins and is also implicated in the pathology of Alzheimer's disease. De novo designed metallo-beta-sheets have been pursued as models and mimics of these proteins. However, no crystal structures of canonical beta-sheet metallopeptides have yet been obtained, in stark contrast to many examples for a-helical metallopeptides, leading to a poor understanding for their chemistry. To address this, we have engineered tryptophan zippers, stable 12-residue beta-sheet peptides, to bind Cu(II) ions and obtained crystal structures through single crystal X-ray diffraction (SC-XRD). We find that metal binding triggers several unexpected supramolecular assemblies that demonstrate the range of higher-order structures available to metallo-beta-sheets. Overall, these findings underscore the importance of crystallography in elucidating the rich structural landscape of metallo-beta-sheet peptides.

Crystallography reveals metal-triggered restructuring of beta-hairpins.,Dang VT, Engineer A, McElheny D, Drena A, Telser J, Tomczak K, Nguyen AI Chemistry. 2024 Aug 16:e202402101. doi: 10.1002/chem.202402101. PMID:39152095<ref>PMID:39152095</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 9bni" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Dang VT]]
[[Category: Nguyen A]]