Energy transduction is the conversion of one form of energy into another; this makes life possible as we know it. Organisms have developed different systems for acquiring energy and storing it in useable forms: the so-called energy currencies. A universal energy currency is the transmembrane difference of electrochemical potential (). This results from the translocation of charges across a membrane, powered by exergonic reactions. Different reactions may be coupled to charge-translocation and, in the majority of cases, these reactions are catalyzed by modular enzymes that always include a transmembrane subunit. The modular arrangement of these enzymes allows for different catalytic and charge-translocating modules to be combined. Thus, a transmembrane charge-translocating module can be associated with different catalytic subunits to form an energy-transducing complex. Likewise, the same catalytic subunit may be combined with a different membrane charge-translocating module. In this work, we analyze the modular arrangement of energy-transducing membrane complexes and discuss their different combinations, focusing on the charge-translocating module.
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December 2021
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Fuelled by the ‘resolution revolution’, cryo-EM has transformed our molecular understanding of transcriptional regulation in bacteria. As an example, Wood and colleagues (pp. 2695–2710) present the sialic acid gene repressor NanR (PDB-6WFG), where cryo-EM revealed the DNA-binding mode. “E. coli Bacteria” by NIAID is licensed under CC BY 2.0. Cover artwork courtesy of Christopher Horne.
Review Article|
December 02 2021
Modularity of membrane-bound charge-translocating protein complexes
Filipa Calisto;
Filipa Calisto
1Instituto de Tecnologia Química e Biológica - António Xavier, Universidade Nova de Lisboa, Av. da República EAN, 2780-157 Oeiras, Portugal
2Faculty of Sciences, Department of Chemistry and Biochemistry and BioISI - Biosystems & Integrative Sciences Institute, University of Lisboa, Campo Grande, 1749-016 Lisboa, Portugal
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Manuela M. Pereira
1Instituto de Tecnologia Química e Biológica - António Xavier, Universidade Nova de Lisboa, Av. da República EAN, 2780-157 Oeiras, Portugal
2Faculty of Sciences, Department of Chemistry and Biochemistry and BioISI - Biosystems & Integrative Sciences Institute, University of Lisboa, Campo Grande, 1749-016 Lisboa, Portugal
Correspondence: Manuela M. Pereira ([email protected])
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Publisher: Portland Press Ltd
Received:
July 30 2021
Revision Received:
November 02 2021
Accepted:
November 15 2021
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2021 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society
2021
Biochem Soc Trans (2021) 49 (6): 2669–2685.
Article history
Received:
July 30 2021
Revision Received:
November 02 2021
Accepted:
November 15 2021
Citation
Filipa Calisto, Manuela M. Pereira; Modularity of membrane-bound charge-translocating protein complexes. Biochem Soc Trans 17 December 2021; 49 (6): 2669–2685. doi: https://doi.org/10.1042/BST20210462
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