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Hybrid Structure of a Dynamic Single-Chain Carboxylase from Deinococcus radiodurans

Hagmann, Anna and Hunkeler, Moritz and Stuttfeld, Edward and Maier, Timm. (2016) Hybrid Structure of a Dynamic Single-Chain Carboxylase from Deinococcus radiodurans. Structure, 24 (8). pp. 1227-1236.

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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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Maier)
UniBasel Contributors:Maier, Timm and Hagmann, Anna and Hunkeler, Moritz and Stuttfeld, Edward
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Cell Press
ISSN:0969-2126
e-ISSN:1878-4186
Note:Publication type according to Uni Basel Research Database: Journal article
Language:English
Identification Number:
Last Modified:11 Jul 2018 12:34
Deposited On:26 Oct 2017 13:03

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