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  In cellulo crystallization of Trypanosoma brucei IMP dehydrogenase enables the identification of genuine co-factors

Nass, K., Redecke, L., Perbandt, M., Yefanov, O., Klinge, M., Koopmann, R., et al. (2020). In cellulo crystallization of Trypanosoma brucei IMP dehydrogenase enables the identification of genuine co-factors. Nature Communications, 11(1): 620, pp. 1-13. doi:10.1038/s41467-020-14484-w.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0005-94E8-E Version Permalink: https://hdl.handle.net/21.11116/0000-0006-05CC-F
Genre: Journal Article

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 Creators:
Nass, Karol, Author
Redecke, Lars, Author
Perbandt, M., Author
Yefanov, O., Author
Klinge, M., Author
Koopmann, R., Author
Stellato, F., Author
Gabdulkhakov, A., Author
Schönherr, R., Author
Rehders, D., Author
Lahey-Rudolph, J. M., Author
Aquila, A., Author
Barty, A., Author
Basu, S., Author
Doak, Bruce1, 2, Author           
Duden, R., Author
Frank, M., Author
Fromme, R., Author
Kassemeyer, Stephan1, 2, Author           
Katona, G., Author
Kirian, R., AuthorLiu, H., AuthorMajoul, I., AuthorMartin-Garcia, J. M., AuthorMesserschmidt, M., AuthorShoeman, Robert L.1, 2, 3, Author           Weierstall, U., AuthorWestenhoff, S., AuthorWhite, T. A., AuthorWilliams, G. J., AuthorYoon, C. H., AuthorZatsepin, N., AuthorFromme, P., AuthorDuszenko, M., AuthorChapman, H. N., AuthorBetzel, C., Author more..
Affiliations:
1Coherent diffractive imaging, Max Planck Institute for Medical Research, Max Planck Society, ou_1497692              
2Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              
3Analytical Protein Biochemistry, Max Planck Institute for Medical Research, Max Planck Society, ou_1497690              

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 Abstract: Sleeping sickness is a fatal disease caused by the protozoan parasite Trypanosoma brucei (Tb). Inosine-5’-monophosphate dehydrogenase (IMPDH) has been proposed as a potential drug target, since it maintains the balance between guanylate deoxynucleotide and ribonucleotide levels that is pivotal for the parasite. Here we report the structure of TbIMPDH at room temperature utilizing free-electron laser radiation on crystals grown in living insect cells. The 2.80 Å resolution structure reveals the presence of ATP and GMP at the canonical sites of the Bateman domains, the latter in a so far unknown coordination mode. Consistent with previously reported IMPDH complexes harboring guanosine nucleotides at the second canonical site, TbIMPDH forms a compact oligomer structure, supporting a nucleotide-controlled conformational switch that allosterically modulates the catalytic activity. The oligomeric TbIMPDH structure we present here reveals the potential of in cellulo crystallization to identify genuine allosteric co-factors from a natural reservoir of specific compounds.

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Language(s): eng - English
 Dates: 2019-05-312020-01-062020-01-30
 Publication Status: Published online
 Pages: 13
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1038/s41467-020-14484-w
URI: https://www.ncbi.nlm.nih.gov/pubmed/32001697
 Degree: -

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Title: Nature Communications
  Abbreviation : Nat. Commun.
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 11 (1) Sequence Number: 620 Start / End Page: 1 - 13 Identifier: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723