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000435344 1001_ $$0P:(DE-H253)PIP1009197$$aNass, Karol$$b0
000435344 245__ $$aIn cellulo crystallization of Trypanosoma brucei IMP dehydrogenase enables the identification of genuine co-factors
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000435344 520__ $$aSleeping sickness is a fatal disease caused by the protozoan parasite Trypanosoma brucei (Tb). Inosine-5’-monophosphate dehydrogenase (IMPDH) has been proposed as a potential drug target, since it maintains the balance between guanylate deoxynucleotide and ribonucleotide levels that is pivotal for the parasite. Here we report the structure of TbIMPDH at room temperature utilizing free-electron laser radiation on crystals grown in living insect cells. The 2.80 Å resolution structure reveals the presence of ATP and GMP at the canonical sites of the Bateman domains, the latter in a so far unknown coordination mode. Consistent with previously reported IMPDH complexes harboring guanosine nucleotides at the second canonical site, TbIMPDH forms a compact oligomer structure, supporting a nucleotide-controlled conformational switch that allosterically modulates the catalytic activity. The oligomeric TbIMPDH structure we present here reveals the potential of in cellulo crystallization to identify genuine allosteric co-factors from a natural reservoir of specific compounds.
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000435344 7001_ $$0P:(DE-H253)PIP1008743$$aRedecke, Lars$$b1
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000435344 7001_ $$00000-0002-7416-6340$$aKoopmann, R.$$b5
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000435344 7001_ $$aLahey-Rudolph, J. M.$$b10
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000435344 7001_ $$0P:(DE-HGF)0$$aDuden, R.$$b15
000435344 7001_ $$0P:(DE-H253)PIP1009688$$aFrank, Matthias$$b16
000435344 7001_ $$0P:(DE-H253)PIP1026130$$aFromme, Raimund$$b17
000435344 7001_ $$0P:(DE-H253)PIP1013003$$aKassemeyer, S.$$b18
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000435344 7001_ $$0P:(DE-H253)PIP1016357$$aKirian, Richard$$b20
000435344 7001_ $$0P:(DE-HGF)0$$aLiu, H.$$b21
000435344 7001_ $$0P:(DE-HGF)0$$aMajoul, I.$$b22
000435344 7001_ $$00000-0002-4558-3858$$aMartin-Garcia, J. M.$$b23
000435344 7001_ $$0P:(DE-H253)PIP1005807$$aMesserschmidt, M.$$b24
000435344 7001_ $$aShoeman, R. L.$$b25
000435344 7001_ $$0P:(DE-H253)PIP1008265$$aWeierstall, U.$$b26
000435344 7001_ $$0P:(DE-H253)PIP1082149$$aWestenhoff, S.$$b27
000435344 7001_ $$0P:(DE-H253)PIP1010779$$aWhite, Thomas$$b28
000435344 7001_ $$0P:(DE-HGF)0$$aWilliams, G. J.$$b29
000435344 7001_ $$0P:(DE-H253)PIP1016300$$aYoon, C. H.$$b30
000435344 7001_ $$0P:(DE-H253)PIP1014437$$aZatsepin, Nadia$$b31
000435344 7001_ $$0P:(DE-H253)PIP1023170$$aFromme, P.$$b32
000435344 7001_ $$0P:(DE-HGF)0$$aDuszenko, M.$$b33
000435344 7001_ $$0P:(DE-H253)PIP1006324$$aChapman, H. N.$$b34
000435344 7001_ $$0P:(DE-H253)PIP1002913$$aBetzel, C.$$b35$$eCorresponding author
000435344 773__ $$0PERI:(DE-600)2553671-0$$a10.1038/s41467-020-14484-w$$gVol. 11, no. 1, p. 620$$n1$$p620$$tNature Communications$$v11$$x2041-1723$$y2020
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