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Ferritin-Like Prote...
Ferritin-Like Proteins : A Conserved Core for a Myriad of Enzyme Complexes
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Banerjee, Rahul (author)
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- Srinivas, Vivek, 1988- (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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- Lebrette, Hugo (author)
- Stockholms universitet,Institutionen för biokemi och biofysik,Université de Toulouse, France
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(creator_code:org_t)
- 2022-09-24
- 2022
- English.
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In: Macromolecular Protein Complexes IV. - Cham : Springer. - 9783031007927 - 9783031007934 ; , s. 109-153
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Subject headings
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- 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.
Subject headings
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
Keyword
- Ferritin-like superfamily
- Methane monooxygenase
- Ribonucleotide reductase
- Aldehyde deformylating oxygenase
- X-ray crystallography
Publication and Content Type
- ref (subject category)
- kap (subject category)
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