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

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

Trypanosoma brucei inosine-5′-monophosphate dehydrogenase (IMPDH) is an enzyme in the guanine nucleotide biosynthesis pathway and of interest as a drug target. Here the authors present the 2.8 Å room temperature structure of TbIMPDH determined by utilizing X-ray free-electron laser radiation and cry...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Karol Nass, Lars Redecke, M. Perbandt, O. Yefanov, M. Klinge, R. Koopmann, F. Stellato, A. Gabdulkhakov, R. Schönherr, D. Rehders, J. M. Lahey-Rudolph, A. Aquila, A. Barty, S. Basu, R. B. Doak, R. Duden, M. Frank, R. Fromme, S. Kassemeyer, G. Katona, R. Kirian, H. Liu, I. Majoul, J. M. Martin-Garcia, M. Messerschmidt, R. L. Shoeman, U. Weierstall, S. Westenhoff, T. A. White, G. J. Williams, C. H. Yoon, N. Zatsepin, P. Fromme, M. Duszenko, H. N. Chapman, C. Betzel
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2020
Materias:
Science
Q
Acceso en línea:https://doaj.org/article/62386f11dbb14a64b2304040fafe13d2
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:62386f11dbb14a64b2304040fafe13d2
record_format dspace
spelling oai:doaj.org-article:62386f11dbb14a64b2304040fafe13d22021-12-02T17:32:43ZIn cellulo crystallization of Trypanosoma brucei IMP dehydrogenase enables the identification of genuine co-factors10.1038/s41467-020-14484-w2041-1723https://doaj.org/article/62386f11dbb14a64b2304040fafe13d22020-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-14484-whttps://doaj.org/toc/2041-1723Trypanosoma brucei inosine-5′-monophosphate dehydrogenase (IMPDH) is an enzyme in the guanine nucleotide biosynthesis pathway and of interest as a drug target. Here the authors present the 2.8 Å room temperature structure of TbIMPDH determined by utilizing X-ray free-electron laser radiation and crystals that were grown in insect cells and find that ATP and GMP are bound at the canonical sites of the Bateman domains.Karol NassLars RedeckeM. PerbandtO. YefanovM. KlingeR. KoopmannF. StellatoA. GabdulkhakovR. SchönherrD. RehdersJ. M. Lahey-RudolphA. AquilaA. BartyS. BasuR. B. DoakR. DudenM. FrankR. FrommeS. KassemeyerG. KatonaR. KirianH. LiuI. MajoulJ. M. Martin-GarciaM. MesserschmidtR. L. ShoemanU. WeierstallS. WestenhoffT. A. WhiteG. J. WilliamsC. H. YoonN. ZatsepinP. FrommeM. DuszenkoH. N. ChapmanC. BetzelNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-13 (2020)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Karol Nass
Lars Redecke
M. Perbandt
O. Yefanov
M. Klinge
R. Koopmann
F. Stellato
A. Gabdulkhakov
R. Schönherr
D. Rehders
J. M. Lahey-Rudolph
A. Aquila
A. Barty
S. Basu
R. B. Doak
R. Duden
M. Frank
R. Fromme
S. Kassemeyer
G. Katona
R. Kirian
H. Liu
I. Majoul
J. M. Martin-Garcia
M. Messerschmidt
R. L. Shoeman
U. Weierstall
S. Westenhoff
T. A. White
G. J. Williams
C. H. Yoon
N. Zatsepin
P. Fromme
M. Duszenko
H. N. Chapman
C. Betzel
In cellulo crystallization of Trypanosoma brucei IMP dehydrogenase enables the identification of genuine co-factors
description Trypanosoma brucei inosine-5′-monophosphate dehydrogenase (IMPDH) is an enzyme in the guanine nucleotide biosynthesis pathway and of interest as a drug target. Here the authors present the 2.8 Å room temperature structure of TbIMPDH determined by utilizing X-ray free-electron laser radiation and crystals that were grown in insect cells and find that ATP and GMP are bound at the canonical sites of the Bateman domains.
format article
author Karol Nass
Lars Redecke
M. Perbandt
O. Yefanov
M. Klinge
R. Koopmann
F. Stellato
A. Gabdulkhakov
R. Schönherr
D. Rehders
J. M. Lahey-Rudolph
A. Aquila
A. Barty
S. Basu
R. B. Doak
R. Duden
M. Frank
R. Fromme
S. Kassemeyer
G. Katona
R. Kirian
H. Liu
I. Majoul
J. M. Martin-Garcia
M. Messerschmidt
R. L. Shoeman
U. Weierstall
S. Westenhoff
T. A. White
G. J. Williams
C. H. Yoon
N. Zatsepin
P. Fromme
M. Duszenko
H. N. Chapman
C. Betzel
author_facet Karol Nass
Lars Redecke
M. Perbandt
O. Yefanov
M. Klinge
R. Koopmann
F. Stellato
A. Gabdulkhakov
R. Schönherr
D. Rehders
J. M. Lahey-Rudolph
A. Aquila
A. Barty
S. Basu
R. B. Doak
R. Duden
M. Frank
R. Fromme
S. Kassemeyer
G. Katona
R. Kirian
H. Liu
I. Majoul
J. M. Martin-Garcia
M. Messerschmidt
R. L. Shoeman
U. Weierstall
S. Westenhoff
T. A. White
G. J. Williams
C. H. Yoon
N. Zatsepin
P. Fromme
M. Duszenko
H. N. Chapman
C. Betzel
author_sort Karol Nass
title In cellulo crystallization of Trypanosoma brucei IMP dehydrogenase enables the identification of genuine co-factors
title_short In cellulo crystallization of Trypanosoma brucei IMP dehydrogenase enables the identification of genuine co-factors
title_full In cellulo crystallization of Trypanosoma brucei IMP dehydrogenase enables the identification of genuine co-factors
title_fullStr In cellulo crystallization of Trypanosoma brucei IMP dehydrogenase enables the identification of genuine co-factors
title_full_unstemmed In cellulo crystallization of Trypanosoma brucei IMP dehydrogenase enables the identification of genuine co-factors
title_sort in cellulo crystallization of trypanosoma brucei imp dehydrogenase enables the identification of genuine co-factors
publisher Nature Portfolio
publishDate 2020
url https://doaj.org/article/62386f11dbb14a64b2304040fafe13d2
work_keys_str_mv AT karolnass incellulocrystallizationoftrypanosomabruceiimpdehydrogenaseenablestheidentificationofgenuinecofactors
AT larsredecke incellulocrystallizationoftrypanosomabruceiimpdehydrogenaseenablestheidentificationofgenuinecofactors
AT mperbandt incellulocrystallizationoftrypanosomabruceiimpdehydrogenaseenablestheidentificationofgenuinecofactors
AT oyefanov incellulocrystallizationoftrypanosomabruceiimpdehydrogenaseenablestheidentificationofgenuinecofactors
AT mklinge incellulocrystallizationoftrypanosomabruceiimpdehydrogenaseenablestheidentificationofgenuinecofactors
AT rkoopmann incellulocrystallizationoftrypanosomabruceiimpdehydrogenaseenablestheidentificationofgenuinecofactors
AT fstellato incellulocrystallizationoftrypanosomabruceiimpdehydrogenaseenablestheidentificationofgenuinecofactors
AT agabdulkhakov incellulocrystallizationoftrypanosomabruceiimpdehydrogenaseenablestheidentificationofgenuinecofactors
AT rschonherr incellulocrystallizationoftrypanosomabruceiimpdehydrogenaseenablestheidentificationofgenuinecofactors
AT drehders incellulocrystallizationoftrypanosomabruceiimpdehydrogenaseenablestheidentificationofgenuinecofactors
AT jmlaheyrudolph incellulocrystallizationoftrypanosomabruceiimpdehydrogenaseenablestheidentificationofgenuinecofactors
AT aaquila incellulocrystallizationoftrypanosomabruceiimpdehydrogenaseenablestheidentificationofgenuinecofactors
AT abarty incellulocrystallizationoftrypanosomabruceiimpdehydrogenaseenablestheidentificationofgenuinecofactors
AT sbasu incellulocrystallizationoftrypanosomabruceiimpdehydrogenaseenablestheidentificationofgenuinecofactors
AT rbdoak incellulocrystallizationoftrypanosomabruceiimpdehydrogenaseenablestheidentificationofgenuinecofactors
AT rduden incellulocrystallizationoftrypanosomabruceiimpdehydrogenaseenablestheidentificationofgenuinecofactors
AT mfrank incellulocrystallizationoftrypanosomabruceiimpdehydrogenaseenablestheidentificationofgenuinecofactors
AT rfromme incellulocrystallizationoftrypanosomabruceiimpdehydrogenaseenablestheidentificationofgenuinecofactors
AT skassemeyer incellulocrystallizationoftrypanosomabruceiimpdehydrogenaseenablestheidentificationofgenuinecofactors
AT gkatona incellulocrystallizationoftrypanosomabruceiimpdehydrogenaseenablestheidentificationofgenuinecofactors
AT rkirian incellulocrystallizationoftrypanosomabruceiimpdehydrogenaseenablestheidentificationofgenuinecofactors
AT hliu incellulocrystallizationoftrypanosomabruceiimpdehydrogenaseenablestheidentificationofgenuinecofactors
AT imajoul incellulocrystallizationoftrypanosomabruceiimpdehydrogenaseenablestheidentificationofgenuinecofactors
AT jmmartingarcia incellulocrystallizationoftrypanosomabruceiimpdehydrogenaseenablestheidentificationofgenuinecofactors
AT mmesserschmidt incellulocrystallizationoftrypanosomabruceiimpdehydrogenaseenablestheidentificationofgenuinecofactors
AT rlshoeman incellulocrystallizationoftrypanosomabruceiimpdehydrogenaseenablestheidentificationofgenuinecofactors
AT uweierstall incellulocrystallizationoftrypanosomabruceiimpdehydrogenaseenablestheidentificationofgenuinecofactors
AT swestenhoff incellulocrystallizationoftrypanosomabruceiimpdehydrogenaseenablestheidentificationofgenuinecofactors
AT tawhite incellulocrystallizationoftrypanosomabruceiimpdehydrogenaseenablestheidentificationofgenuinecofactors
AT gjwilliams incellulocrystallizationoftrypanosomabruceiimpdehydrogenaseenablestheidentificationofgenuinecofactors
AT chyoon incellulocrystallizationoftrypanosomabruceiimpdehydrogenaseenablestheidentificationofgenuinecofactors
AT nzatsepin incellulocrystallizationoftrypanosomabruceiimpdehydrogenaseenablestheidentificationofgenuinecofactors
AT pfromme incellulocrystallizationoftrypanosomabruceiimpdehydrogenaseenablestheidentificationofgenuinecofactors
AT mduszenko incellulocrystallizationoftrypanosomabruceiimpdehydrogenaseenablestheidentificationofgenuinecofactors
AT hnchapman incellulocrystallizationoftrypanosomabruceiimpdehydrogenaseenablestheidentificationofgenuinecofactors
AT cbetzel incellulocrystallizationoftrypanosomabruceiimpdehydrogenaseenablestheidentificationofgenuinecofactors
_version_ 1718380188977332224

Ejemplares similares