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Crystal structure of unphosphorylated Spo0F from Paenisporosarcina sp. TG-14, a psychrophilic bacterium isolated from an Antarctic glacier

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Title
Crystal structure of unphosphorylated Spo0F from Paenisporosarcina sp. TG-14, a psychrophilic bacterium isolated from an Antarctic glacier
Other Titles
남극 빙하 미생물 유래 스포어 형성관련 단백질인 PaSpo0F 의 삼차구조 연구
Authors
Lee, Chang Sup
Jeong, Chang Sook
Park, Sun-Ha
Lee, Chang Woo
Lee, Jun Hyuck
Park, HaJeung
Park, Hyun
Park, Hyun Ho
Hong, Jong Wook
Keywords
Paenisporosarcina sp. TG-14; Spo0F; X-ray crystallography; crystal structure; spore formation
Issue Date
2018-12
Citation
Lee, Chang Sup, et al. 2018-12. "Crystal structure of unphosphorylated Spo0F from Paenisporosarcina sp. TG-14, a psychrophilic bacterium isolated from an Antarctic glacier". Biodesign, 6(4): 84-91.
Abstract
Spo0F is a response regulator that modulates sporulation, undergoes phosphorylation for phosphorelay signal transduction, and interacts with various regulatory proteins; however, the mechanisms through which phosphorylation induces structural changes and regulates interactions with binding partners remain unclear. Here, we determined the unphosphorylated crystal structure of Spo0F from the psychrophilic bacterium Paenisporosarcina sp. TG-14 (PaSpo0F) and established a phosphorylation-state structural model. We found that PaSpo0F underwent structural changes (Lys54 and Lys102) by phosphorylation and generated new interactions (Lys102/Gln10 and Lys54/Glu84) to stabilize the β4/α4 and β1/α1 loop structures, which are important target-protein binding sites. Analysis of Bacillus subtilis Spo0 variants revealed movement by BsSpo0F Thr82 and Tyr84 residues following interaction with BsSpo0B, providing insight into the movement of corresponding residues in PaSpo0F (Thr80 and Tyr82), with further analysis of BsSpo0F/BsRapH interaction revealing alterations in the β4/α4 loop region. These results suggest that phosphorylation-induced structural rearrangement might be essential for PaSpo0F activation and expand the understanding of Spo0F-specific activation mechanisms during sporulation.
URI
https://repository.kopri.re.kr/handle/201206/9622
ISSN
2288-6982
Other Identifiers
eISSN 2288-7105
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