6b5w

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'''Unreleased structure'''
 
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The entry 6b5w is ON HOLD
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==Benenodin-1-dC5, state 2==
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<StructureSection load='6b5w' size='340' side='right'caption='[[6b5w]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6b5w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Asticcacaulis_benevestitus_DSM_16100_=_ATCC_BAA-896 Asticcacaulis benevestitus DSM 16100 = ATCC BAA-896]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5tj0 5tj0]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6B5W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6B5W FirstGlance]. <br>
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</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=6b5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b5w OCA], [https://pdbe.org/6b5w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6b5w RCSB], [https://www.ebi.ac.uk/pdbsum/6b5w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6b5w ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/V4RMX4_9CAUL V4RMX4_9CAUL]
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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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Authors: Link, J.A., Zong, C.
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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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Description: Benenodin-1-dC5, state 2
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Link, J.A]]
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<div class="pdbe-citations 6b5w" style="background-color:#fffaf0;"></div>
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[[Category: Zong, C]]
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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: Asticcacaulis benevestitus DSM 16100 = ATCC BAA-896]]
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[[Category: Large Structures]]
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[[Category: Link AJ]]
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[[Category: Zong C]]

Current revision

Benenodin-1-dC5, state 2

PDB ID 6b5w

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