Ontology highlight
ABSTRACT:
SUBMITTER: Sharma P
PROVIDER: S-EPMC5773532 | biostudies-literature | 2018 Jan
REPOSITORIES: biostudies-literature
Sharma Pankaj P Maklashina Elena E Cecchini Gary G Iverson T M TM
Nature communications 20180118 1
Flavin is covalently attached to the protein scaffold in ~10% of flavoenzymes. However, the mechanism of covalent modification is unclear, due in part to challenges in stabilizing assembly intermediates. Here, we capture the structure of an assembly intermediate of the Escherichia coli Complex II (quinol:fumarate reductase (FrdABCD)). The structure contains the E. coli FrdA subunit bound to covalent FAD and crosslinked with its assembly factor, SdhE. The structure contains two global conformatio ...[more]