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TitleMolecular and Low-Resolution Structural Characterization of the Na-Translocating Glutaconyl-CoA Decarboxylase From .
Journal, issue, pagesFront Microbiol, Vol. 11, Page 480, Year 2020
Publish dateMar 31, 2020
AuthorsStella Vitt / Simone Prinz / Nils Hellwig / Nina Morgner / Ulrich Ermler / Wolfgang Buckel /
PubMed AbstractSome 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 linksFront Microbiol / PubMed:32300335 / PubMed Central
MethodsEM (single particle)
Resolution15.0 Å
Structure data

EMDB-10743:
Low resolution structure of Glutaconyl-CoA Decarboxylase from Clostridium symbiosum
Method: EM (single particle) / Resolution: 15.0 Å

Source
  • Clostridium symbiosum (bacteria)

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