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Structural insights into the psychrophilic germinal protease PaGPR and its autoinhibitory loop

Cited 2 time in wos
Cited 2 time in scopus
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Title
Structural insights into the psychrophilic germinal protease PaGPR and its autoinhibitory loop
Other Titles
남극 빙하미생물 유래 germinal protease (PaGPR) 의 구조 연구
Authors
Lee, Chang Woo
Lee, Saeyoung
Jeong, Chang Sook
Hwang, Jisub
Chang, Jeong Ho
Choi, In-Geol
Kim, T. Doohun
Park, HaJeung
Kim, Hye-Yeon
Lee, Jun Hyuck
Subject
Microbiology
Keywords
crystal structure; germination protease; X-ray crystallography; zymogen
Issue Date
2020-09
Citation
Lee, Chang Woo, et al. 2020. "Structural insights into the psychrophilic germinal protease PaGPR and its autoinhibitory loop". JOURNAL OF MICROBIOLOGY, 58(9): 772-779.
Abstract
In spore forming microbes, germination protease (GPR) plays a key role in the initiation of the germination process. A critical step during germination is the degradation of small acid-soluble proteins (SASPs), which protect spore DNA from external stresses (UV, heat, low temperature, etc.). Inactive zymogen GPR can be activated by autoprocessing of the N-terminal pro-sequence domain. Activated GPR initiates the degradation of SASPs; however, the detailed mechanisms underlying the activation, catalysis, regulation, and substrate recognition of GPR remain elusive. In this study, we determined the crystal structure of GPR fromPaenisporosarcinasp. TG-20 (PaGPR) in its inactive form at a resolution of 2.5 A. Structural analysis showed that the active site of PaGPR is sterically occluded by an inhibitory loop region (residues 202-216). The N-terminal region interacts directly with the self-inhibitory loop region, suggesting that the removal of the N-terminal pro-sequence induces conformational changes, which lead to the release of the self-inhibitory loop region from the active site. In addition, comparative sequence and structural analyses revealed thatPaGPR contains two highly conserved Asp residues (D123 and D182) in the active site, similar to the putative aspartic acid protease GPR fromBacillus megaterium.The catalytic domain structure of PaGPR also shares similarities with the sequentially non-homologous proteins HycI and HybD. HycI and HybD are metal-loproteases that also contain two Asp (or Glu) residues in their active site, playing a role in metal binding. In summary, our results provide useful insights into the activation process ofPaGPR and its active conformation.
URI
https://repository.kopri.re.kr/handle/201206/11890
DOI
http://dx.doi.org/10.1007/s12275-020-0292-0
Appears in Collections  
2020-2020, Post-Polar Genomics Project: Functional genomic study for securing of polar useful genes (20-20) / Kim, Jin-Hyoung (PE20040)
2020-2020, Development of potential candidates as antibiotics based on polar genetic resources (20-20) / Lee, Jun Hyuck (PM20030)
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