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  Molecular and Low-Resolution Structural Characterization of the Na+-Translocating Glutaconyl-CoA Decarboxylase From Clostridium symbiosum

Vitt, S., Prinz, S., Hellwig, N., Morgner, N., Ermler, U., & Buckel, W. (2020). Molecular and Low-Resolution Structural Characterization of the Na+-Translocating Glutaconyl-CoA Decarboxylase From Clostridium symbiosum. Frontiers in Microbiology, 11: 480. doi:10.3389/fmicb.2020.00480.

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 Creators:
Vitt, Stella1, 2, Author              
Prinz, Simone3, 4, Author              
Hellwig, Nils5, Author
Morgner, Nina5, Author
Ermler, Ulrich1, Author              
Buckel, Wolfgang2, Author
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Faculty of Biology, Philipps-Universität Marburg, Marburg, Germany, ou_persistent22              
3Central Electron Microscopy Facility, Max Planck Institute of Biophysics, Max Planck Society, ou_3249263              
4Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, Max-von-Laue-Straße 3, 60438 Frankfurt am Main, DE, ou_2068291              
5Institute of Physical and Theoretical Chemistry, Goethe University Frankfurt, Frankfurt, Germany, ou_persistent22              

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Free keywords: anaerobic energy metabolism; glutaconyl-CoA decarboxylase; ion translocation; biotin; negative-stain electron microscopy; LILBID-MS
 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 (Gcd), a member of this protein family, drives the endergonic translocation of Na+ across the membrane with the exergonic decarboxylation of glutaconyl-CoA (ΔG0’ ≈−30 kJ/mol) to crotonyl-CoA. Here, we report on the molecular characterization of Gcd from Clostridium symbiosum 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.

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Language(s): eng - English
 Dates: 2019-12-092020-03-052020-03-31
 Publication Status: Published online
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.3389/fmicb.2020.00480
 Degree: -

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Title: Frontiers in Microbiology
  Abbreviation : Front. Microbiol.
Source Genre: Journal
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Publ. Info: Lausanne : Frontiers Media
Pages: - Volume / Issue: 11 Sequence Number: 480 Start / End Page: - Identifier: ISSN: 1664-302X
CoNE: https://pure.mpg.de/cone/journals/resource/1664-302X