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Crystal structure of the inactive state of the receiver domain of Spo0A from Paenisporosarcina sp. TG-14, a psychrophilic bacterium isolated from an Antarctic glacier

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Title
Crystal structure of the inactive state of the receiver domain of Spo0A from Paenisporosarcina sp. TG-14, a psychrophilic bacterium isolated from an Antarctic glacier
Other Titles
남극 빙하에서 발견된 호냉성 박테리아 (Paenisporosarcina sp. TG-14) 유래의 스포어 형성 관련 단백질인 Spo0A receiver domain 의 삼차구조 연구
Authors
Lee, Chang Woo
Lee, Jun Hyuck
HaJeung Park
Park, Hyun
Hak Jun Kim
Sunghwan Kim
Hyun Ho Park
Kim, Han-Woo
Han, Se Jong
Shin, Seung Chul
Lee, Sung Gu
Park, Sun-Ha
Subject
Microbiology
Keywords
Analytical ultracentrifugation; Paenisporosarcina sp. TG-14; Spo0A; Spore formation; X-ray crystallography
Issue Date
2017
Citation
Lee, Chang Woo, et al. 2017. "Crystal structure of the inactive state of the receiver domain of Spo0A from Paenisporosarcina sp. TG-14, a psychrophilic bacterium isolated from an Antarctic glacier". JOURNAL OF MICROBIOLOGY, 55(6): 464-474.
Abstract
The two-component phosphorelay system is the most prevalent mechanism for sensing and transducing environmental signals in bacteria. Spore formation, which relies on the two-component phosphorelay system, enables the long-term survival of the glacial bacterium Paenisporosarcina sp. TG-14 in the extreme cold environment. Spo0A is a key response regulator of the phosphorelay system in the early stage of spore formation. The protein is composed of a regulatory N-terminal phospho-receiver domain and a DNA-binding C-terminal activator domain. We solved the three-dimensional structure of the unphosphorylated (inactive) form of the receiver domain of Spo0A (PaSpo0A-R) from Paenisporosarcina sp. TG-14. A structural comparison with phosphorylated (active form) Spo0A from Bacillus stearothermophilus (BsSpo0A) showed minor notable differences. A molecular dynamics study of a model of the active form and the crystal structures revealed significant differences in the α4 helix and the preceding loop region where phosphorylation occurs. Although an oligomerization study of PaSpo0A-R by analytical ultracentrifugation (AUC) has shown that the protein is in a monomeric state in solution, both crosslinking and crystal-packing analyses indicate the possibility of weak dimer formation by a previously undocumented mechanism. Collectively, these observations provide insight into the mechanism of phosphorylation-dependent activation unique to Spo0A.
URI
http://repository.kopri.re.kr/handle/201206/6187
DOI
http://dx.doi.org/10.1007/s12275-017-6599-9
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