Mimicry of ice structure by surface hydroxyls and water of a β-helix antifreeze protein

@article{Liou2000MimicryOI,
  title={Mimicry of ice structure by surface hydroxyls and water of a $\beta$-helix antifreeze protein},
  author={Y. Liou and A. Tocilj and P. Davies and Z. Jia},
  journal={Nature},
  year={2000},
  volume={406},
  pages={322-324}
}
Insect antifreeze proteins (AFP) are much more effective than fish AFPs at depressing solution freezing points by ice-growth inhibition. [...] Key Result Not only are the 12-amino-acid loops almost identical in the backbone, but also the conserved side chains are positioned in essentially identical orientations, making this AFP perhaps the most regular protein structure yet observed. The protein has almost no hydrophobic core but is stabilized by numerous disulphide and hydrogen bonds.Expand
β-Helix structure and ice-binding properties of a hyperactive antifreeze protein from an insect
TLDR
The solution structure of spruce budworm AFP is reported and its ice-binding properties are characterized; the 9-kDa AFP is a β-helix with a triangular cross-section and rectangular sides that form stacked parallel β-sheets; a fold which is distinct from the three known fish AFP structures. Expand
The structure and function of b-helical antifreeze proteins
TLDR
Comparisons of the newly determined ryegrass and carrot AFP sequences have led to models suggesting that they might also consist of b-helices, and indicate that the b-helix might be used as an AFP structural motif in nonfish. Expand
Ice-binding site of snow mold fungus antifreeze protein deviates from structural regularity and high conservation
TLDR
The 0.95-Å high-resolution crystal structure of a 223-residue secreted AFP from the snow mold fungus Typhula ishikariensis is reported, which is remarkable for its lack of regularity and its poor conservation in homologs from psychrophilic diatoms and bacteria and other fungi. Expand
Crystal structure of an insect antifreeze protein reveals ordered waters on the ice-binding surface.
TLDR
This work has solved the crystal structure at 2.05-Å resolution of an AFP from the longhorn beetle, Rhagium mordax with five molecules in the unit cell that is hyperactive and has a β-solenoid fold with a wide, flat ice-binding surface formed by four parallel rows of mainly Thr residues. Expand
Novel dimeric β-helical model of an ice nucleation protein with bridged active sites
TLDR
Dimerization dramatically increases the 'ice-active' surface area of theprotein by doubling its width, increasing its length, and presenting identical ice-forming surfaces on both sides of the protein, suggesting that this allows sufficient anchored clathrate waters to align on the INP surface to nucleate freezing. Expand
Crystal structure of beta-helical antifreeze protein points to a general ice binding model.
TLDR
The CfAFP structure led us to reevaluate the authors' ice binding model, and the analysis of three possible modes of docking gives rise to a binding mechanism based on surface complementarity that is applicable to both fish and insect AFPs. Expand
Structural basis of antifreeze activity of a bacterial multi-domain antifreeze protein
TLDR
The crystal structure of the first multi-domain AFP that has been characterized provides a molecular basis for understanding differences in antifreeze activity between the two domains of this protein and general insight on how structural differences in the ice-binding sites affect the activity of AFPs. Expand
Cold survival in freeze-intolerant insects: the structure and function of beta-helical antifreeze proteins.
TLDR
Comparisons of the newly determined ryegrass and carrot AFP sequences have led to models suggesting that they might also consist of beta-helices, and indicate that the beta-helix might be used as an AFP structural motif in nonfish organisms. Expand
Anchored clathrate waters bind antifreeze proteins to ice
TLDR
The mechanism by which antifreeze proteins irreversibly bind to ice has been elucidated through solving the first crystal structure of an Antarctic bacterial AFP, which folds as a Ca2+-bound parallel beta-helix with an extensive array of ice-like surface waters that are anchored via hydrogen bonds directly to the polypeptide backbone and adjacent side chains. Expand
Cold survival in freeze‐intolerant insects
TLDR
Comparisons of the newly determined ryegrass and carrot AFP sequences have led to models suggesting that they might also consist of β-helices, and indicate that the β-helix might be used as an AFP structural motif in nonfish organisms. Expand
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β-Helix structure and ice-binding properties of a hyperactive antifreeze protein from an insect
TLDR
The solution structure of spruce budworm AFP is reported and its ice-binding properties are characterized; the 9-kDa AFP is a β-helix with a triangular cross-section and rectangular sides that form stacked parallel β-sheets; a fold which is distinct from the three known fish AFP structures. Expand
Ice-binding structure and mechanism of an antifreeze protein from winter flounder
TLDR
An ice-binding model is proposed that accounts for the binding specificity of the antifreeze protein along the <011¯2> axes of the {202¯1} ice planes1. Expand
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NMR analysis and secondary structure predictions agree with the CD data and are consistent with a beta-helix model proposed for the antifreeze on the basis of its 12-amino-acid repeating structure and presumptive disulfide bond arrangement. Expand
Mapping of disulfide bridges in antifreeze proteins from overwintering larvae of the beetle Dendroides canadensis.
TLDR
This study demonstrated that all of the 16 Cys residues in the Dendroides AFPs are disulfide bridged, and the location of cysteines every six residues throughout their length is essential to understanding the structure of these AFPs. Expand
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Experimental results show that fish antifreeze glycopeptides 8 and 7 bond onto ice prism planes aligned along a-axes, and inhibit crystal growth on prism planes and on surfaces close to that orientation, explaining why the chemical adsorption is virtually irreversible and the crystal growth can be stopped virtually completely. Expand
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It is suggested that the stacking of the coils and the unusual near perpendicular junction of PB2 and PB3 make the parallel β-helix fold especially likely to maintain similar main chain conformations during divergent evolution even after all vestige of similarity in primary structure has vanished. Expand
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TLDR
Genomic Southern blots suggest there may be 30-50 tightly linked copies of the gene, which is a signature consistently seen with unrelated fish antifreeze protein genes, and one that has been associated with the need to rapidly increase gene product in response to climate change. Expand
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TLDR
It is suggested that the stacking of the coils and the unusual near perpendicular junction of PB2 and PB3 make the parallel beta-helix fold especially likely to maintain similar main chain conformations during divergent evolution even after all vestige of similarity in primary structure has vanished. Expand
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The crystal structure of a dipeptide complex of bovine neurophysin II has been solved at 2.8 A resolution solely by using single-wavelength anomalous scattering data from a single iodinatedExpand
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The tailspike protein (TSP) of Salmonella typhimurium phage P22 is a part of the apparatus by which the phage attaches to the bacterial host and hydrolyzes the O antigen. It has served as a modelExpand
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