학술논문
In cellulo crystallization of Trypanosoma brucei IMP dehydrogenase enables the identification of genuine co-factors
Document Type
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
Source
Nature Communications, Vol 11, Iss 1, Pp 1-13 (2020)
Subject
Language
English
ISSN
2041-1723
Abstract
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.