The crystal structure of mouse IRG1 suggests that cis-aconitate decarboxylase has an open and closed conformation

Hye Lin Chun; So Yeon Lee; Ki-Hwa Kim; Chang Sup Lee; Tae-Jin Oh; Hyun Ho Park

doi:10.1371/journal.pone.0242383

The crystal structure of mouse IRG1 suggests that cis-aconitate decarboxylase has an open and closed conformation

PLoS One. 2020 Dec 1;15(12):e0242383. doi: 10.1371/journal.pone.0242383. eCollection 2020.

Authors

Hye Lin Chun¹, So Yeon Lee¹, Ki-Hwa Kim², Chang Sup Lee³, Tae-Jin Oh^{2

4

5}, Hyun Ho Park¹

Affiliations

¹ College of Pharmacy, Chung-Ang University, Seoul, Republic of Korea.
² Department of Life Science and Biochemical Engineering, Graduate School, SunMoon University, Asan, Republic of Korea.
³ College of Pharmacy and Research Institute of Pharmaceutical Science, Gyeongsang National University, Jinju, Republic of Korea.
⁴ Genome-based BioIT Convergence Institute, Asan, Republic of Korea.
⁵ Department of Pharmaceutical Engineering and Biotechnology, SunMoon University, Asan, Republic of Korea.

Abstract

Coordinate and structural factors were deposited with the Protein Data Bank under PDB ID: 7BR9.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Aconitic Acid / chemistry
Amino Acid Sequence / genetics
Animals
Carboxy-Lyases / chemistry
Carboxy-Lyases / genetics
Carboxy-Lyases / ultrastructure*
Crystallography, X-Ray
Databases, Protein
Hydro-Lyases / chemistry
Hydro-Lyases / genetics
Hydro-Lyases / ultrastructure*
Mice
Models, Molecular
Protein Conformation*

Substances

Aconitic Acid
Carboxy-Lyases
aconitate decarboxylase
Hydro-Lyases
Irg1 protein, mouse

Grants and funding

This study was supported by the Basic Science Research Program of the National Research Foundation of Korea (NRF), funded by the Korea government (MSIT) (grant no. NRF-2017M3A9D8062960 and NRF-2018R1A4A1023822, both to HHP).