Crystal Structure and Mutational Analysis of Ca2+-Independent Type II Antifreeze Protein from Longsnout Poacher, Brachyopsis rostratus

Nishimiya, Yoshiyuki; Kondo, Hidemasa; Takamichi, Manabu; Sugimoto, Hiroshi; Suzuki, Mamoru; Miura, Ai; Tsuda, Sakae

doi:10.1016/j.jmb.2008.07.042

Cited by 67 publications

(64 citation statements)

References 67 publications

(124 reference statements)

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“…An earlier study using 13 Ca relaxation experiments suggested that the C-terminal Thr 35 and Arg 37 might be more flexible than other parts of HPLC6, but the weak signal due to the use of natural abundance carbon prevented a definitive statement from being made. 28 We show here that there is a moderate increase in the flexibility at the C-terminus of Type I AFP HPLC6, demonstrating that a correctly positioned Thr 35 methyl group on the Ala-rich face is not critical for activity.…”

Section: Discussionmentioning

confidence: 99%

“…How the AFP binds to the ice surface has been more difficult to determine as there are no consistently conserved motifs in AFP protein sequences or structures. The known and predicted structural folds include a single a-helical structure (Type I AFP), 11 lectin folds (Type II AFP), 12,13 mixed irregular a-helix and b-strand (Type III AFP), 14,15 a-helical bundle (Type IV AFP), 16 b-helical fold (some insect and plant AFPs), [17][18][19] and polyproline Type II fold (snow flea AFP). 20,21 The structures of Types II-IV AFPs and the insect AFPs are reviewed in Refs.…”

Section: Introductionmentioning

confidence: 99%

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Increased flexibility decreases antifreeze protein activity

Patel

Graether

2010

Protein Science

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Antifreeze proteins protect several cold-blooded organisms from subzero environments by preventing death from freezing. The Type I antifreeze protein (AFP) isoform from Pseudopleuronectes americanus, named HPLC6, is a 37-residue protein that is a single a-helix. Mutational analysis of the protein showed that its alanine-rich face is important for binding to and inhibiting the growth of macromolecular ice. Almost all structural studies of HPLC6 involve the use of chemically synthesized protein as it requires a native N-terminal aspartate and an amidated C-terminus for full activity. Here, we examine the role of C-terminal amide and C-terminal arginine side chain in the activity, structure, and dynamics of nonamidated Arg 37 HPLC6, nonamidated HPLC6 Ala 37 , amidated HPLC6 Ala 37 , and fully native HPLC6 using a recombinant bacterial system. The thermal hysteresis (TH) activities of the nonamidated mutants are 35% lower compared with amidated proteins, but analysis of the NMR data and circular dichroism spectra shows that they are all still a-helical. Relaxation data from the two nonamidated mutants indicate that the C-terminal residues are considerably more flexible than the rest of the protein because of the loss of the amide group, whereas the amidated Ala 37 mutant has a C-terminus that is as rigid as the wild-type protein and has high TH activity. We propose that an increase in flexibility of the AFP causes it to lose activity because its dynamic nature prevents it from binding strongly to the ice surface.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Increased flexibility decreases antifreeze protein activity

Patel

Graether

2010

Protein Science

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“…47,48 In contrast, type II and III fish AFPs are nonrepetitive and show an overall globular fold. 49,50 In fish type II AFPs, this fold is stabilized by cysteine residues. Herring hAFP-II has five intramolecular cysteine bridges and binds one Ca 2þ ion [ Fig.…”

Section: Structure Of Ice-binding Proteinsmentioning

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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“…AFPs have been isolated from a variety of organisms and classified into several groups (types I-IV, insect AFPs, bacterial AFPs, and plant AFPs) depending on their structural characteristics and source (15)(16)(17)(18)(19)(20)(21)(22)(23)(24)(25). Although each antifreeze class differs dramatically in its sequences and structures and even binds to different planes of ice, the various classes do have some properties in common (2,3,26).…”

mentioning

confidence: 99%

“…To date, NMR and crystal structures of AFPs from polar fish (15)(16)(17)(18)(19)(20), insects (22,23), and psychrophilic bacteria (21) have been reported. The structures of insect and bacterial AFPs exhibit a ␤-helical fold, and these proteins have a regular pattern of Thr residues.…”

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confidence: 99%

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

Lee

Park

et al. 2012

Journal of Biological Chemistry

122

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Background: Ice-binding proteins improve the cold tolerance of cells by inhibiting ice growth and recrystallization. Results: Crystal structure and mutagenesis data of LeIBP suggests the B face as an ice-binding site. Conclusion: LeIBP structure adopts a ␤-helical fold and the aligned Thr/Ser/Ala residues are critical for ice binding. Significance: LeIBP structure can serve as a structural model for a large number of IBPs.

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Crystal Structure and Mutational Analysis of Ca2+-Independent Type II Antifreeze Protein from Longsnout Poacher, Brachyopsis rostratus

Cited by 67 publications

References 67 publications

Increased flexibility decreases antifreeze protein activity

Increased flexibility decreases antifreeze protein activity

Interaction of ice binding proteins with ice, water and ions

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

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