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Proc. Natl. Acad. Sci. USA, Apr 23 2024, 121 (17) | https://doi.org/10.1073/pnas.2320312121
Structural insights into the regulation of protein-arginine kinase McsB by McsA
Md Arifuzzamana, Eunju Kwonb,c,1, and Dong Young Kima,1
aCollege of Pharmacy, Yeungnam University, Gyeongsan 38541, Republic of Korea;
bDivision of Life Science, Gyeongsang National University, Jinju 52828, Republic of Korea; and
cResearch Institute of Molecular Alchemy, Gyeongsang National University, Jinju 52828, Republic of Korea
1To whom correspondence may be addressed. : Eunju Kwon, Dong Young Kim
Abstract
In gram-positive bacteria, phosphorylated arginine functions as a protein degradation signal in a similar manner as ubiquitin in eukaryotes. The protein-arginine phosphorylation is mediated by the McsAB complex, where McsB possesses kinase activity and McsA modulates McsB activity. Although
mcsA and
mcsB are regulated within the same operon, the role of McsA in kinase activity has not yet been clarified. In this study, we determined the molecular mechanism by which McsA regulates kinase activity. The crystal structure of the McsAB complex shows that McsA binds to the McsB kinase domain through a second zinc-coordination domain and the subsequent loop region. This binding activates McsB kinase activity by rearranging the catalytic site, preventing McsB self-assembly, and enhancing stoichiometric substrate binding. The first zinc-coordination and coiled-coil domains of McsA further activate McsB by reassembling the McsAB oligomer. These results demonstrate that McsA is the regulatory subunit for the reconstitution of the protein-arginine kinase holoenzyme. This study provides structural insight into how protein-arginine kinase directs the cellular protein degradation system.
논문정보
- Research article
- 2024년 04월 (BRIC 등록일 2024-04-17)
- 국내 연구진
- 생명과학 > 구조생물 및 생물물리학
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