6b5w | pdb_00006b5w

Benenodin-1-dC5, state 2

spinqualitylabelsall models 6b5w Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6b5w is a 1 chain structure with sequence from Asticcacaulis benevestitus DSM 16100 = ATCC BAA-896. This structure supersedes the now removed PDB entry 5tj0. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function V4RMX4_9CAUL Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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