title: The ring residue proline 8 is crucial for the thermal stability of the lasso peptide caulosegnin II.
abstract: Lasso peptides are fascinating natural products with a unique structural fold that can exhibit tremendous thermal stability. Here, we investigate factors responsible for the thermal stability of caulosegnin II. By employing X-ray crystallography, mutational analysis and molecular dynamics simulations, the ring residue proline 8 was proven to be crucial for thermal stability.
authors: Department of Chemistry/Biochemistry, LOEWE Center for Synthetic Microbiology, Philipps-Universität Marburg, Hans-Meerwein-Strasse 4, 35032 Marburg, Germany. marahiel@staff.uni-marburg.de.
authors: Julian D
authors: JD
authors: Hegemann
authors: Christopher D
authors: CD
authors: Fage
authors: Shaozhou
authors: S
authors: Zhu
authors: Klaus
authors: K
authors: Harms
authors: Francesco Saverio
authors: FS
authors: Di Leva
authors: Ettore
authors: E
authors: Novellino
authors: Luciana
authors: L
authors: Marinelli
authors: Mohamed A
authors: MA
authors: Marahiel
mesh_terms: D000595:Amino Acid Sequence; D008958:Models, Molecular; D008968:Molecular Conformation; D005810:Multigene Family; D010455:Peptides / Q000737:chemistry* / Q000235:genetics; D011392:Proline / Q000737:chemistry*; D055550:Protein Stability; D013816:Thermodynamics
chemical_list: D010455:Peptides; C581445:caulosegnin II; D011392:Proline