5FIF

Carboxyltransferase domain of a single-chain bacterial carboxylase

Summary for 5FIF

• Entry DOI: 10.2210/pdb5fif/pdb
• Descriptor: Carboxylase, 1,2-ETHANEDIOL (3 entities in total)
• Functional Keywords: multienzymes, protein dynamics, small-angle x-ray scattering, carrier protein, ligase
• Biological source: Deinococcus radiodurans
• Total number of polymer chains: 6
• Total formula weight: 359552.34

Authors

Hagmann, A.,Hunkeler, M.,Stuttfeld, E.,Maier, T. (deposition date: 2015-12-23, release date: 2016-07-20, Last modification date: 2024-01-10)

Primary citation

Hagmann, A.,Hunkeler, M.,Stuttfeld, E.,Maier, T.
Hybrid Structure of a Dynamic Single-Chain Carboxylase from Deinococcus radiodurans.
Structure, 24:1227-1236, 2016

PubMed Abstract: 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.

PubMed: 27396827
DOI: 10.1016/j.str.2016.06.001

Experimental method

X-RAY DIFFRACTION (2.494 Å)