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Cryo-EM reveals architecture and domain interactions of putative tumor suppressor ALDH1L1, a product of natural fusion of three unrelated genes

Published online by Cambridge University Press:  30 July 2021

Yaroslav Tsybovsky ,
Valentin Sereda  and
Sergey Krupenko
Yaroslav Tsybovsky
Affiliation:
Frederick National Laboratory for Cancer Research, Frederick, Maryland, United States
Valentin Sereda
Affiliation:
UNC Chapel Hill, United States
Sergey Krupenko
Affiliation:
UNC Chapel Hill, United States

Abstract

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Type
3D Structures: From Macromolecular Assemblies to Whole Cells (3DEM FIG)
Information
Microscopy and Microanalysis , Volume 27 , Supplement S1 , August 2021 , pp. 1118 - 1119
Copyright
Copyright © The Author(s), 2021. Published by Cambridge University Press on behalf of the Microscopy Society of America

References

Krupenko, SA. FDH: an aldehyde dehydrogenase fusion enzyme in folate metabolism. Chem Biol Interact. 2009;178(1-3):84-93.CrossRefGoogle ScholarPubMed
Donato, H, Krupenko, NI, Tsybovsky, Y, Krupenko, SA. 10-formyltetrahydrofolate dehydrogenase requires a 4'-phosphopantetheine prosthetic group for catalysis. J Biol Chem. 2007;282(47):34159-66.CrossRefGoogle Scholar
Chumanevich, AA, Krupenko, SA, Davies, C. The crystal structure of the hydrolase domain of 10-formyltetrahydrofolate dehydrogenase: mechanism of hydrolysis and its interplay with the dehydrogenase domain. J Biol Chem. 2004;279(14):14355-64.CrossRefGoogle ScholarPubMed
Tsybovsky, Y, Donato, H, Krupenko, NI, Davies, C, Krupenko, SA. Crystal structures of the carboxyl terminal domain of rat 10-formyltetrahydrofolate dehydrogenase: implications for the catalytic mechanism of aldehyde dehydrogenases. Biochemistry. 2007;46(11):2917-29.CrossRefGoogle ScholarPubMed