Antibody Probes of Module 1 of the 6-Deoxyerythronolide B Synthase Reveal an Extended Conformation During Ketoreduction.

ABSTRACT: The 6-deoxyerythronolide B synthase (DEBS) is a prototypical assembly line polyketide synthase (PKS) that synthesizes the macrocyclic core of the antibiotic erythromycin. Each of its six multidomain modules presumably sample distinct conformations, as biosynthetic intermediates tethered to their acyl carrier proteins interact with multiple active sites during the courses of their catalytic cycles. The spatiotemporal details underlying these protein dynamics remain elusive. Here, we investigate one aspect of this conformational flexibility using two domain-specific monoclonal antibody fragments (F_abs) isolated from a very large naïve human antibody library. Both F_abs, designated 1D10 and 2G10, were bound specifically and with high affinity to the ketoreductase domain o

SUBMITTER: Cogan DP 

PROVIDER: S-EPMC7484051 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature