Wazir, S., Maksimainen, M. M., & Lehtiö, L. (2020). Multiple crystal forms of human MacroD2. Acta Crystallographica Section F Structural Biology Communications, 76(10), 477–482. https://doi.org/10.1107/s2053230x20011309
Multiple crystal forms of human MacroD2
|Author:||Wazir, Sarah1; Maksimainen, Mirko M.1; Lehtiö, Lari1|
1Faculty of Biochemistry and Molecular Medicine, University of Oulu, P.O.Box 5400, Oulu, Finland, 90014, Finland
|Online Access:||PDF Full Text (PDF, 1.3 MB)|
|Persistent link:|| http://urn.fi/urn:nbn:fi-fe2020120399311
John Wiley & Sons,
|Publish Date:|| 2020-12-03
MacroD2 is one of the three human macrodomain proteins characterized by their protein-linked mono-ADP-ribosyl-hydrolyzing activity. MacroD2 is a single-domain protein that contains a deep ADP-ribose-binding groove. In this study, new crystallization conditions for MacroD2 were found and three crystal structures of human MacroD2 in the apo state were solved in space groups P4₁2₁2, P43212 and P4₃, and refined at 1.75, 1.90 and 1.70 Å resolution, respectively. Structural comparison of the apo crystal structures with the previously reported crystal structure of MacroD2 in complex with ADP-ribose revealed conformational changes in the side chains of Val101, Ile189 and Phe224 induced by the binding of ADP-ribose in the active site. These conformational variations may potentially facilitate design efforts of a MacroD2 inhibitor.
Acta crystallographica. Section F, Structural biology communications
|Pages:||477 - 482|
|Type of Publication:||
A1 Journal article – refereed
|Field of Science:||
1182 Biochemistry, cell and molecular biology
This work was funded by Academy of Finland (grant Nos.287063 and 294085) and by the Sigrid Juse ́lius Foundation.
|Academy of Finland Grant Number:||
287063 (Academy of Finland Funding decision)
294085 (Academy of Finland Funding decision)
© 2020 International Union of Crystallography. The final authenticated version is available online at https://doi.org/10.1107/s2053230x20011309.