Download MendeleyA high-resolution structure that provides insight into coiled-coil thiodepsipeptide dynamic chemistry
Dadon, Z., Samiappan, M., Shahar, A., Zarivach, R., Ashkenasy, G.(2013) Angew Chem Int Ed Engl 52: 9944-9947
- PubMed: 23929823
- DOI: https://doi.org/10.1002/anie.201303900
- Primary Citation of Related Structures:
3W8V, 3W92, 3W93 - PubMed Abstract:
Stable and reactive: A crystal structure at 1.35 ? of a thioester coiled-coil protein reveals high similarity to all-peptide-bond proteins. In these assemblies, the thioester bonds are kept reactive towards thiol molecules in the mixture. This enables efficient domain exchange between proteins in response to changes in folding conditions or introduction of external templates.
Organizational Affiliation:
Department of Chemistry, Ben Gurion University of the Negev, Beer Sheva, 84105 (Israel).
