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Title | Molecular and Low-Resolution Structural Characterization of the Na-Translocating Glutaconyl-CoA Decarboxylase From . |
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Journal, issue, pages | Front Microbiol, Vol. 11, Page 480, Year 2020 |
Publish date | Mar 31, 2020 |
Authors | Stella Vitt / Simone Prinz / Nils Hellwig / Nina Morgner / Ulrich Ermler / Wolfgang Buckel / |
PubMed Abstract | Some anaerobic bacteria use biotin-dependent Na-translocating decarboxylases (Bdc) of β-keto acids or their thioester analogs as key enzymes in their energy metabolism. Glutaconyl-CoA decarboxylase ...Some anaerobic bacteria use biotin-dependent Na-translocating decarboxylases (Bdc) of β-keto acids or their thioester analogs as key enzymes in their energy metabolism. Glutaconyl-CoA decarboxylase (Gcd), a member of this protein family, drives the endergonic translocation of Na across the membrane with the exergonic decarboxylation of glutaconyl-CoA (Δ ' ≈-30 kJ/mol) to crotonyl-CoA. Here, we report on the molecular characterization of Gcd from based on native PAGE, size exclusion chromatography (SEC) and laser-induced liquid bead ion desorption mass spectrometry (LILBID-MS). The obtained molecular mass of ca. 400 kDa fits to the DNA sequence-derived mass of 379 kDa with a subunit composition of 4 GcdA (65 kDa), 2 GcdB (35 kDa), GcdC1 (15 kDa), GcdC2 (14 kDa), and 2 GcdD (10 kDa). Low-resolution structural information was achieved from preliminary electron microscopic (EM) measurements, which resulted in a 3D reconstruction model based on negative-stained particles. The Gcd structure is built up of a membrane-spanning base primarily composed of the GcdB dimer and a solvent-exposed head with the GcdA tetramer as major component. Both globular parts are bridged by a linker presumably built up of segments of GcdC1, GcdC2 and the 2 GcdDs. The structure of the highly mobile Gcd complex represents a template for the global architecture of the Bdc family. |
External links | Front Microbiol / PubMed:32300335 / PubMed Central |
Methods | EM (single particle) |
Resolution | 15.0 Å |
Structure data | EMDB-10743: |
Source |
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