Ferritin-Like Proteins: A Conserved Core for a Myriad of Enzyme Complexes

Banerjee, Rahul; Srinivas, Vivek; Lebrette, Hugo

doi:10.1007/978-3-031-00793-4_4

Part of the book series: Subcellular Biochemistry ((SCBI,volume 99))

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Abstract

Ferritin-like proteins share a common fold, a four α-helix bundle core, often coordinating a pair of metal ions. Although conserved, the ferritin fold permits a diverse set of reactions, and is central in a multitude of macromolecular enzyme complexes. Here, we emphasize this diversity through three members of the ferritin-like superfamily: the soluble methane monooxygenase, the class I ribonucleotide reductase and the aldehyde deformylating oxygenase. They all rely on dinuclear metal cofactors to catalyze different challenging oxygen-dependent reactions through the formation of multi-protein complexes. Recent studies using cryo-electron microscopy, serial femtosecond crystallography at an X-ray free electron laser source, or single-crystal X-ray diffraction, have reported the structures of the active protein complexes, and revealed unprecedented insights into the molecular mechanisms of these three enzymes.

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Authors and Affiliations

Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN, USA
Rahul Banerjee
Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden
Vivek Srinivas & Hugo Lebrette
Laboratoire de Microbiologie et Génétique Moléculaires (LMGM), Centre de Biologie Intégrative (CBI), CNRS, UPS, Université de Toulouse, Toulouse, France
Hugo Lebrette

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Rahul Banerjee
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Vivek Srinivas
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Hugo Lebrette
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Correspondence to Hugo Lebrette .

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Institute of Molecular Physiology, University of Mainz, Mainz, Germany
J. Robin Harris
Biosciences Institute, Newcastle University, Newcastle upon Tyne, UK
Jon Marles-Wright

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Banerjee, R., Srinivas, V., Lebrette, H. (2022). Ferritin-Like Proteins: A Conserved Core for a Myriad of Enzyme Complexes. In: Harris, J.R., Marles-Wright, J. (eds) Macromolecular Protein Complexes IV. Subcellular Biochemistry, vol 99. Springer, Cham. https://doi.org/10.1007/978-3-031-00793-4_4

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DOI: https://doi.org/10.1007/978-3-031-00793-4_4
Published: 24 September 2022
Publisher Name: Springer, Cham
Print ISBN: 978-3-031-00792-7
Online ISBN: 978-3-031-00793-4
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