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A High‐Resolution Structure that Provides Insight into Coiled‐Coil Thiodepsipeptide Dynamic Chemistry
Author(s) -
Dadon Zehavit,
Samiappan Manickasundaram,
Shahar Anat,
Zarivach Raz,
Ashkenasy Gonen
Publication year - 2013
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201303900
Subject(s) - thioester , coiled coil , folding (dsp implementation) , chemistry , nanotechnology , computer science , domain (mathematical analysis) , high resolution , computational biology , biochemistry , materials science , engineering , biology , geography , mathematical analysis , remote sensing , mathematics , electrical engineering , enzyme
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.