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| - | | + | #REDIRECT [[6b5w]] This PDB entry is obsolete and replaced by 6b5w |
| - | ==Benenodin-1-dC5, state 2==
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| - | <StructureSection load='5tj0' size='340' side='right' caption='[[5tj0]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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| - | == Structural highlights ==
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| - | <table><tr><td colspan='2'>[[5tj0]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TJ0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TJ0 FirstGlance]. <br>
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| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5tj1|5tj1]]</td></tr>
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5tj0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tj0 OCA], [http://pdbe.org/5tj0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tj0 RCSB], [http://www.ebi.ac.uk/pdbsum/5tj0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tj0 ProSAT]</span></td></tr>
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| - | </table>
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| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | Mechanically interlocked molecules that change their conformation in response to stimuli have been developed by synthetic chemists as building blocks for molecular machines. Here we describe a natural product, the lasso peptide benenodin-1, which exhibits conformational switching between two distinct threaded conformers upon actuation by heat. We have determined the structures of both conformers and have characterized the kinetics and energetics of the conformational switch. Single amino acid substitutions to benenodin-1 generate peptides that are biased to a single conformer, showing that the switching behavior is potentially an evolvable trait in these peptides. Lasso peptides such as benenodin-1 can be recognized and cleaved by enzymes called lasso peptide isopeptidases. We show that only the native conformer of benenodin-1 is cleaved by its cognate isopeptidase. Thus, thermally induced conformational switching of benenodin-1 may also be relevant to the biological function of these molecules.
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| - | Lasso Peptide Benenodin-1 Is a Thermally Actuated [1]Rotaxane Switch.,Zong C, Wu MJ, Qin JZ, Link AJ J Am Chem Soc. 2017 Aug 2;139(30):10403-10409. doi: 10.1021/jacs.7b04830. Epub, 2017 Jul 24. PMID:28696674<ref>PMID:28696674</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 5tj0" style="background-color:#fffaf0;"></div>
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| - | == References ==
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| - | <references/>
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| - | __TOC__
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| - | </StructureSection>
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| - | [[Category: Link, A J]]
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| - | [[Category: Zong, C]]
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| - | [[Category: Lasso peptide ripp]]
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| - | [[Category: Unknown function]]
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