A high-resolution structure that provides insight into coiled-coil thiodepsipeptide dynamic chemistry.
Stable and reactive: A crystal structure at 1.35 Å 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.
Department of Chemistry, Ben Gurion University of the Negev, Beer Sheva, 84105 (Israel).
Zehavit
Z
Dadon
Manickasundaram
M
Samiappan
Anat
A
Shahar
Raz
R
Zarivach
Gonen
G
Ashkenasy
D000595:Amino Acid Sequence; D047630:Depsipeptides / Q000096:biosynthesis / Q000737:chemistry*; D008958:Models, Molecular; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
D047630:Depsipeptides; D011506:Proteins
coiled coils; depsipeptides; dynamic chemistry; peptide networks; thiodepsipeptides