Structural Basis for Antifreeze Activity of Ice-binding Protein from Arctic Yeast

Lee, Jun Hyuck; Park, Ae Kyung; Do, Hackwon; Park, Kyoung Sun; Moh, Sang Hyun; Min, Young; Kim, Soo Hyun

doi:10.1074/jbc.m111.331835

Cited by 95 publications

(124 citation statements)

References 46 publications

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“…The six β-helical loops are of different lengths ranging from 18 to 27 residues, with the number of residues constructing each loop given in parentheses as follows: β1, V15-G32 (18); β6, R206-K223 (18); β5, T188-G205 (18); β4, K167-G187 (21); β3, D140-A166 (27); β2, P117-T139 (23). The minimum length of the loop appears to be 18 residues, as seen in the three consecutive loops (β1, β6, and β5) at the top of the molecule.…”

Section: Resultsmentioning

confidence: 99%

Ice-binding site of snow mold fungus antifreeze protein deviates from structural regularity and high conservation

Kondo

Hanada

Sugimoto

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

138

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Antifreeze proteins (AFPs) are found in organisms ranging from fish to bacteria, where they serve different functions to facilitate survival of their host. AFPs that protect freeze-intolerant fish and insects from internal ice growth bind to ice using a regular array of well-conserved residues/motifs. Less is known about the role of AFPs in freeze-tolerant species, which might be to beneficially alter the structure of ice in or around the host. Here we report the 0.95-Å high-resolution crystal structure of a 223-residue secreted AFP from the snow mold fungus Typhula ishikariensis. Its main structural element is an irregular β-helix with six loops of 18 or more residues that lies alongside an α-helix. β-Helices have independently evolved as AFPs on several occasions and seem ideally structured to bind to several planes of ice, including the basal plane. A novelty of the β-helical fold is the nonsequential arrangement of loops that places the N-and C termini inside the solenoid of β-helical coils. The ice-binding site (IBS), which could not be predicted from sequence or structure, was located by site-directed mutagenesis to the flattest surface of the protein. It is remarkable for its lack of regularity and its poor conservation in homologs from psychrophilic diatoms and bacteria and other fungi.X-ray crystallography | ice growth inhibition | thermal hysteresis

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Section: Resultsmentioning

confidence: 99%

Ice-binding site of snow mold fungus antifreeze protein deviates from structural regularity and high conservation

Kondo

Hanada

Sugimoto

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

138

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“…An a-helix lies alongside the b-helix axis. [59][60][61] Yet other IBP structures are found in insect RiAFP and sfAFP. The structure of RiAFP of the beetle Rhagium inquisitor is formed by two closely packed b-sheets [ Fig.…”

Section: -58mentioning

confidence: 99%

“…Despite this lack regularity in the IBS these proteins are able to bind both basal and prism planes. [59][60][61]65 Crystal structures of various AFPs reveal ordered waters associated with the protein IBS, 48,56,58,65 which are thought to play an important role in ice-binding (see Sec. VI E for more details).…”

Section: -58mentioning

confidence: 99%

Interaction of ice binding proteins with ice, water and ions

et al. 2016

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Articles you may be interested inExplicit-water theory for the salt-specific effects and Hofmeister series in protein solutions J. Chem. Phys. 144, 215101 (2016) Ice binding proteins (IBPs) are produced by various cold-adapted organisms to protect their body tissues against freeze damage. First discovered in Antarctic fish living in shallow waters, IBPs were later found in insects, microorganisms, and plants. Despite great structural diversity, all IBPs adhere to growing ice crystals, which is essential for their extensive repertoire of biological functions. Some IBPs maintain liquid inclusions within ice or inhibit recrystallization of ice, while other types suppress freezing by blocking further ice growth. In contrast, ice nucleating proteins stimulate ice nucleation just below 0 C. Despite huge commercial interest and major scientific breakthroughs, the precise working mechanism of IBPs has not yet been unraveled. In this review, the authors outline the state-of-the-art in experimental and theoretical IBP research and discuss future scientific challenges. The interaction of IBPs with ice, water and ions is examined, focusing in particular on ice growth inhibition mechanisms.

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“…본 연구팀은 북극 효모 Glaciozyma sp. AY30으로부터 약 25kDa의 결빙방지단백질 LeIBP (Leucosporidium icebinding protein)을 분리하여 특성 및 대량생산 연구를 수행하 였다 [8][9][10][11]. 또한, 본 연구팀에서는 남극 호냉성 세균 Flavobacterium frigoris PS1으로부터 결빙방지단백질 (FfIBP)을 분 리하여 LeIBP와 얼음 결합능을 분자 구조적인 관점에서 비 교하였고 [12], 재조합 Pichia pastoris를 이용하여 유가식 배 양을 통해 생산최적화를 수행한 결과 FfIBP는 LeIBP과 유사 한 3차원 구조를 가짐에도 불구하고 LeIBP의 0.42°C 보다 두 배정도 높은 0.85°C의 TH 활성을 보였다 [13] .…”

Section: Introductionunclassified

Pilot-scale Production of the Antifreeze Protein from Antarctic Bacterium Flavobacterium frigoris PS1 by Recombinant Escherichia coli with a Cold Shock Induction System

Kim¹,

Lee²,

Lee³

et al. 2015

KSBB Journal

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Antifreeze proteins (AFP) inhibit growth and recrystallization of ice, and permit organisms to survive in cold environments. The AFP from an Antarctic bacterium, Flavobacterium frigoris PS1, FfIBP (Flavobacterium frigoris icebinding protein), was produced in E. coli using a cold shock induction system. The culture temperature was shifted from 37°C to 15°C and a 20 L culture scale was used. The final weights of dried cell and FfIBP were estimated to be 126 g and 8.4 g, respectively. The thermal hysteresis (TH) activity (1.53°C) of the produced FfIBP was 3.6-fold higher than that of the LeIBP (Leucosporidium ice-binding protein) produced in Picha. The current study demonstrates that large-scale production of FfIBP was successful and the result could be extended to further application studies using recombinant AFPs.

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Structural Basis for Antifreeze Activity of Ice-binding Protein from Arctic Yeast

Cited by 95 publications

References 46 publications

Ice-binding site of snow mold fungus antifreeze protein deviates from structural regularity and high conservation

Ice-binding site of snow mold fungus antifreeze protein deviates from structural regularity and high conservation

Interaction of ice binding proteins with ice, water and ions

Pilot-scale Production of the Antifreeze Protein from Antarctic Bacterium Flavobacterium frigoris PS1 by Recombinant Escherichia coli with a Cold Shock Induction System

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