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Crystallization and preliminary X-ray crystallographic analysis of an ice-binding protein (FfIBP) from Flavobacterium frigoris PS1

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Title
Crystallization and preliminary X-ray crystallographic analysis of an ice-binding protein (FfIBP) from Flavobacterium frigoris PS1
Other Titles
남극 호냉성 박테리아 Flavobacterium frigoris PS1 유래 결빙방지단백질 (FfIBP) 의 결정화 및 삼차구조 해석을 위한 X-선 회절데이타 분석
Authors
Lee, Jun Hyuck
Do, Hackwon
Kim, Hak Jun
Lee, Sung Gu
Subject
Biochemistry & Molecular Biology; Biophysics; Crystallography
Keywords
Antifreeze protein; Flavobacterium frigoris PS1; X-ray protein crystallography; crystal structure; ice-binding protein
Issue Date
2012
Publisher
International Union of Crystallography
Citation
Lee, Jun Hyuck, et al. 2012. "Crystallization and preliminary X-ray crystallographic analysis of an ice-binding protein (FfIBP) from Flavobacterium frigoris PS1". ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 68: 806-809.
Abstract
Ice growth in a cold environment is fatal for polar organisms, not only because of the physical destruction of inner cell organelles but also because of the resulting chemical damage due to processes such as osmotic shock. The properties of ice-binding proteins (IBPs), which include antifreeze proteins (AFPs), have been characterized, and IBPs exhibit the ability to inhibit ice growth by binding to specific ice planes and lowering the freezing point. Our lab has recently succeeded in over-expressing an ice-binding protein (FfIBP) from the Gram-negative bacteria Flavobacterium frigoris PS1, which was isolated from the Antarctic. Interestingly, the thermal hysteresis activity of FfIBP was approximately 2.5°C at 50 ?M, which is 10 times higher than that of the moderately active IBP from Arctic yeast (LeIBP). Although FfIBP closely resembles LeIBP in its amino acid sequence, the antifreeze activity of FfIBP appears to be much greater than that of LeIBP. In an effort to understand the reason for this difference, we attempted to solve the crystal structure of FfIBP. Herein, the crystallization methods and X-ray diffraction data for FfIBP are reported. FfIBP was crystallized using the hanging drop vapor diffusion method with 0.1 M sodium acetate at pH 4.4 and 3 M sodium chloride as a precipitant. A complete diffraction data set was collected at a resolution of 2.9 ?. The crystal belos of ice-binding proteins (IBPs), which include antifreeze proteins (AFPs), have been characterized, and IBPs exhibit the ability to inhibit ice growth by binding to specific ice planes and lowering the freezing point. Our lab has recently succeeded in over-expressing an ice-binding protein (FfIBP) from the Gram-negative bacteria Flavobacterium frigoris PS1, which was isolated from the Antarctic. Interestingly, the thermal hysteresis activity of FfIBP was approximately 2.5°C at 50 ?M, which is 10 times higher than that of the moderately active IBP from Arctic yeast (LeIBP)
URI
http://repository.kopri.re.kr/handle/201206/6395
DOI
http://dx.doi.org/10.1107/S1744309112020465
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