KOPRI Repository

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

Cited 0 time in wos
Cited 0 time in scopus

Full metadata record

DC Field Value Language
dc.contributor.authorLee, Chang Sup-
dc.contributor.authorJeong, Chang Sook-
dc.contributor.authorPark, Sun-Ha-
dc.contributor.authorLee, Chang Woo-
dc.contributor.authorLee, Jun Hyuck-
dc.contributor.authorPark, HaJeung-
dc.contributor.authorPark, Hyun-
dc.contributor.authorPark, Hyun Ho-
dc.contributor.authorHong, Jong Wook-
dc.date.accessioned2019-08-14T07:36:22Z-
dc.date.available2019-08-14T07:36:22Z-
dc.date.issued2018-12-
dc.identifiereISSN 2288-7105-
dc.identifier.issn2288-6982-
dc.identifier.urihttps://repository.kopri.re.kr/handle/201206/9622-
dc.description.abstractSpo0F 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.en_US
dc.formatapplication/pdf-
dc.languageengligh-
dc.subject.classificationKing Sejong Stationen_US
dc.titleCrystal structure of unphosphorylated Spo0F from Paenisporosarcina sp. TG-14, a psychrophilic bacterium isolated from an Antarctic glacieren_US
dc.title.alternative남극 빙하 미생물 유래 스포어 형성관련 단백질인 PaSpo0F 의 삼차구조 연구en_US
dc.typeArticleen_US
dc.identifier.bibliographicCitationLee, Chang Sup, et al. 2018. "Crystal structure of unphosphorylated Spo0F from Paenisporosarcina sp. TG-14, a psychrophilic bacterium isolated from an Antarctic glacier". <em>Biodesign</em>, 6(4): 84-91.-
dc.citation.titleBiodesignen_US
dc.citation.volume6en_US
dc.citation.number4en_US
dc.citation.startPage84en_US
dc.citation.endPage91en_US
dc.description.articleClassificationKCI등재후보-
dc.description.jcrRateJCR 2016:0en_US
dc.subject.keywordPaenisporosarcina sp. TG-14en_US
dc.subject.keywordSpo0Fen_US
dc.subject.keywordX-ray crystallographyen_US
dc.subject.keywordcrystal structureen_US
dc.subject.keywordspore formationen_US
dc.identifier.localId2018-0421-
Appears in Collections  
2018-2018, Development of potential candidates as antibiotics based on polar genetic resources (18-18) / Lee, Jun Hyuck (PE18210)
2019-2019, Development of potential candidates as antibiotics based on polar genetic resources (19-19) / Lee, Jun Hyuck (PE19210)
Files in This Item

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

Browse