Multiple crystal forms of human MacroD2
Sarah Wazir, Mirko M. Maksimainen and Lari Lehtiö [1]
Molecular Tour
MacroD2 is one of the three human macrodomain proteins characterized for their protein linked mono-ADP-ribosyl-hydrolyzing activity. MacroD2 is a single domain protein containing a deep ADP-ribose binding groove. In this study new crystallization conditions for MacroD2 were found and three crystal structures of human MacroD2 in apo state were solved in space groups P41212, P43212 and P43 and refined at 1.75, 1.90 and 1.70 Å resolutions, respectively. Structural comparison of the apo crystal structures to the previously reported MacroD2 crystal structure in complex with ADP-ribose revealed conformational changes in the side chains of Val101, Ile189 and Phe224 induced by the binding of ADP-ribose into the active site. These conformational variations may potentially facilitate design efforts of a MacroD2 inhibitor.
Ribbon representations of the secondary structures of apo MacroD2 in:
- (PDB ID 6y4y, chain A) (light blue).
- (PDB ID 6y4z, chain A) (warm pink).
- (PDB ID 6y73, chain A) (salmon).
References
- ↑ Wazir S, Maksimainen MM, Lehtio L. Multiple crystal forms of human MacroD2. Acta Crystallogr F Struct Biol Commun. 2020 Oct 1;76(Pt 10):477-482. doi:, 10.1107/S2053230X20011309. Epub 2020 Sep 15. PMID:33006575 doi:http://dx.doi.org/10.1107/S2053230X20011309
