title: Capturing the Structure of the Substrate Bound Condensation Domain.
abstract: Condensation domains of nonribosomal peptide synthetase machineries have so far escaped detailed structural analysis. In this issue of Cell Chemical Biology, Bloudoff et al. (2016) describe a protein tethering technique that allowed the authors to obtain structural information on the substrate bound state of the first condensation domain from calcium-dependent antibiotic biosynthesis, thus opening a new window into how these important biosynthetic machineries function.
authors.affiliation: Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany.
authors.forename: Tiia
authors.initials: T
authors.lastname: Kittilä
authors.affiliation: Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany; EMBL Australia Monash University, Clayton, VIC 3800, Australia; The Department of Biochemistry and Molecular Biology and ARC Centre of Excellence in Advanced Molecular Imaging, Monash University, 15 Innovation Walk, Clayton, VIC 3800, Australia. Electronic address: max.cryle@monash.edu.
authors.forename: Max J
authors.initials: MJ
authors.lastname: Cryle
mesh_terms: D010453:Peptide Synthases / Q000737:chemistry*
chemical_list: D010453:Peptide Synthases