A High‐Resolution Structure that Provides Insight into Coiled‐Coil Thiodepsipeptide Dynamic Chemistry1. Issue 38 (8th August 2013)

• Record Type: Journal Article
• Authors: Dadon, Zehavit; Samiappan, Manickasundaram; Shahar, Anat; Zarivach, Raz; Ashkenasy, Gonen
• Is Part Of: Angewandte Chemie international edition. Volume 52:Issue 38(2013)
• Page Start: 9944
• Page End: 9947
• Publication Date: 2013-08-08
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201303900
• Languages: English
• ISSNs: 1433-7851

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>Stable and reactive</bold>: 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.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg37r9mkbt" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>