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Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella

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Published on: November 30, 2018

Multiple crystal forms of human MacroD2.

Sarah Wazir¹, Mirko M Maksimainen¹, Lari Lehtiö¹

¹Faculty of Biochemistry and Molecular Medicine, University of Oulu, PO Box 5400, Oulu 90014, Finland.

Acta Crystallographica. Section F, Structural Biology Communications

|October 2, 2020

Summary

This summary is machine-generated.

Researchers determined the apo crystal structures of MacroD2, a protein involved in mono-ADP-ribosyl hydrolysis. Structural analysis revealed conformational changes upon ADP-ribose binding, aiding potential inhibitor design.

Keywords:

ADP-ribosyl-hydrolase ADP-ribosylation apo structure crystal forms macrodomain

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Last Updated: Dec 7, 2025

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Published on: March 28, 2011

Area of Science:

Biochemistry
Structural Biology
Enzymology

Background:

MacroD2 is one of three human proteins with mono-ADP-ribosyl-hydrolyzing activity.
It possesses a single domain featuring a distinct ADP-ribose-binding groove.

Purpose of the Study:

To determine new crystallization conditions for human MacroD2.
To solve and refine crystal structures of MacroD2 in its apo state.
To analyze conformational changes induced by ADP-ribose binding.

Main Methods:

X-ray crystallography was employed to obtain high-resolution crystal structures.
Three apo crystal structures of MacroD2 were solved in space groups P41212, P43212, and P43.
Structures were refined at resolutions of 1.75, 1.90, and 1.70 Å.

Main Results:

New crystallization conditions for MacroD2 were successfully identified.
Three distinct apo crystal structures of human MacroD2 were determined.
Conformational changes in key residues (Val101, Ile189, Phe224) were observed upon ADP-ribose binding.

Conclusions:

The solved apo structures provide insights into MacroD2's structural dynamics.
Observed conformational variations are crucial for understanding enzyme-substrate interactions.
These findings may guide the rational design of MacroD2 inhibitors.