5D9E

Crystal Structure of the Proline-rich Lasso Peptide Caulosegnin II

Summary for 5D9E

• Entry DOI: 10.2210/pdb5d9e/pdb
• Descriptor: Caulosegnin II, CHLORIDE ION (3 entities in total)
• Functional Keywords: lasso peptide, unknown function
• Biological source: Caulobacter segnis
• Total number of polymer chains: 1
• Total formula weight: 2051.71

Authors

Fage, C.D.,Hegemann, J.D.,Harms, K.,Marahiel, M.A. (deposition date: 2015-08-18, release date: 2016-02-17, Last modification date: 2025-04-09)

Primary citation

Hegemann, J.D.,Fage, C.D.,Zhu, S.,Harms, K.,Di Leva, F.S.,Novellino, E.,Marinelli, L.,Marahiel, M.A.
The ring residue proline 8 is crucial for the thermal stability of the lasso peptide caulosegnin II.
Mol Biosyst, 12:1106-1109, 2016

PubMed 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.

PubMed: 26863937
DOI: 10.1039/c6mb00081a

Experimental method

X-RAY DIFFRACTION (0.859 Å)