6B58
FrdA-SdhE assembly intermediate
Summary for 6B58
| Entry DOI | 10.2210/pdb6b58/pdb |
| Descriptor | Fumarate reductase flavoprotein subunit, FAD assembly factor SdhE, FLAVIN-ADENINE DINUCLEOTIDE, ... (10 entities in total) |
| Functional Keywords | frda, flavoprotein, assembly intermediate, complex, respiration |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 4 |
| Total formula weight | 149180.94 |
| Authors | Sharma, P.,Iverson, T.M. (deposition date: 2017-09-28, release date: 2018-01-24, Last modification date: 2023-11-15) |
| Primary citation | Sharma, P.,Maklashina, E.,Cecchini, G.,Iverson, T.M. Crystal structure of an assembly intermediate of respiratory Complex II. Nat Commun, 9:274-274, 2018 Cited by PubMed Abstract: 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 conformational changes as compared to prior structures of the mature protein: the rotation of a domain within the FrdA subunit, and the destabilization of two large loops of the FrdA subunit, which may create a tunnel to the active site. We infer a mechanism for covalent flavinylation. As supported by spectroscopic and kinetic analyses, we suggest that SdhE shifts the conformational equilibrium of the FrdA active site to disfavor succinate/fumarate interconversion and enhance covalent flavinylation. PubMed: 29348404DOI: 10.1038/s41467-017-02713-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.611 Å) |
Structure validation
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