TY - JOUR
T1 - Capturing the Structure of the Substrate Bound Condensation Domain
AU - Kittila, Tiia
AU - Cryle, Max J.
PY - 2016/3/17
Y1 - 2016/3/17
N2 - 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.
AB - 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.
UR - http://www.ncbi.nlm.nih.gov/pubmed/26991098
U2 - 10.1016/j.chembiol.2016.03.003
DO - 10.1016/j.chembiol.2016.03.003
M3 - Editorial
SN - 1074-5521
VL - 23
SP - 315
EP - 316
JO - Chemistry and Biology
JF - Chemistry and Biology
IS - 3
ER -