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Publication Abstract from PubMed

Biotin-dependent acyl-coenzyme A (CoA) carboxylases (aCCs) are involved in key steps of anabolic pathways and comprise three distinct functional units: biotin carboxylase (BC), biotin carboxyl carrier protein (BCCP), and carboxyl transferase (CT). YCC multienzymes are a poorly characterized family of prokaryotic aCCs of unidentified substrate specificity, which integrate all functional units into a single polypeptide chain. We employed a hybrid approach to study the dynamic structure of Deinococcus radiodurans (Dra) YCC: crystal structures of isolated domains reveal a hexameric CT core with extended substrate binding pocket and a dimeric BC domain. Negative-stain electron microscopy provides an approximation of the variable positioning of the BC dimers relative to the CT core. Small-angle X-ray scattering yields quantitative information on the ensemble of Dra YCC structures in solution. Comparison with other carrier protein-dependent multienzymes highlights a characteristic range of large-scale interdomain flexibility in this important class of biosynthetic enzymes.

Hybrid Structure of a Dynamic Single-Chain Carboxylase from Deinococcus radiodurans.,Hagmann A, Hunkeler M, Stuttfeld E, Maier T Structure. 2016 Jul 6. pii: S0969-2126(16)30120-4. doi:, 10.1016/j.str.2016.06.001. PMID:27396827^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.