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Heme-binding enables allosteric modulation in an ancient TIM-barrel glycosidase
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- Gamiz-Arco, Gloria (författare)
- Univ Granada, Fac Ciencias, Dept Quim Fis, Unidad Excelencia Quim Aplicada Biomed & Medioamb, E-18071 Granada, Spain.
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- Gutierrez-Rus, Luis I. (författare)
- Univ Granada, Fac Ciencias, Dept Quim Fis, Unidad Excelencia Quim Aplicada Biomed & Medioamb, E-18071 Granada, Spain.
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- Risso, Valeria A. (författare)
- Univ Granada, Fac Ciencias, Dept Quim Fis, Unidad Excelencia Quim Aplicada Biomed & Medioamb, E-18071 Granada, Spain.
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- Univ Granada, Fac Ciencias, Dept Quim Fis, Unidad Excelencia Quim Aplicada Biomed & Medioamb, E-18071 Granada, Spain Georgia State Univ, Dept Biol, Atlanta, GA 30303 USA. (creator_code:org_t)
- 2021-01-15
- 2021
- Engelska.
- Ingår i: Nature Communications. - : Springer Nature. - 2041-1723. ; 12
- Tidskriftsartikel (refereegranskat)
Abstract
Ämnesord
Stäng
- Glycosidases are phylogenetically widely distributed enzymes that are crucial for the cleavage of glycosidic bonds. Here, we present the exceptional properties of a putative ancestor of bacterial and eukaryotic family-1 glycosidases. The ancestral protein shares the TIM-barrel fold with its modern descendants but displays large regions with greatly enhanced conformational flexibility. Yet, the barrel core remains comparatively rigid and the ancestral glycosidase activity is stable, with an optimum temperature within the experimental range for thermophilic family-1 glycosidases. None of the similar to 5500 reported crystallographic structures of similar to 1400 modern glycosidases show a bound porphyrin. Remarkably, the ancestral glycosidase binds heme tightly and stoichiometrically at a well-defined buried site. Heme binding rigidifies this TIM-barrel and allosterically enhances catalysis. Our work demonstrates the capability of ancestral protein reconstructions to reveal valuable but unexpected biomolecular features when sampling distant sequence space. The potential of the ancestral glycosidase as a scaffold for custom catalysis and biosensor engineering is discussed. Family 1 glycosidases (GH1) are present in the three domains of life and share classical TIM-barrel fold. Structural and biochemical analyses of a resurrected ancestral GH1 enzyme reveal heme binding, not known in its modern descendants. Heme rigidifies the TIM-barrel and allosterically enhances catalysis.
Ämnesord
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
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