3nla: Difference between revisions

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==Overview==

Antifreeze proteins (AFPs) have the unique ability to adsorb to ice and, inhibit its growth. Many organisms ranging from fish to bacteria use AFPs, to retard freezing or lessen the damage incurred upon freezing and, thawing. The ice-binding mechanism of the long linear alpha-helical type I, AFPs has been attributed to their regularly spaced polar residues matching, the ice lattice along a pyramidal plane. In contrast, it is not known how, globular antifreeze proteins such as type III AFP that lack repeating, ice-binding residues bind to ice. Here we report the 1.25 A crystal, structure of recombinant type III AFP (QAE isoform) from eel pout, (Macrozoarces americanus), which reveals a remarkably flat amphipathic, ice-binding site where five hydrogen-bonding atoms match two ranks of, oxygens on the [1010] ice prism plane in the <0001> direction, giving high, ice-binding affinity and specificity. This binding site, substantiated by, the structures and properties of several ice-binding site mutants, suggests that the AFP occupies a niche in the ice surface in which it, covers the basal plane while binding to the prism face.

Antifreeze proteins (AFPs) have the unique ability to adsorb to ice and inhibit its growth. Many organisms ranging from fish to bacteria use AFPs to retard freezing or lessen the damage incurred upon freezing and thawing. The ice-binding mechanism of the long linear alpha-helical type I AFPs has been attributed to their regularly spaced polar residues matching the ice lattice along a pyramidal plane. In contrast, it is not known how globular antifreeze proteins such as type III AFP that lack repeating ice-binding residues bind to ice. Here we report the 1.25 A crystal structure of recombinant type III AFP (QAE isoform) from eel pout (Macrozoarces americanus), which reveals a remarkably flat amphipathic ice-binding site where five hydrogen-bonding atoms match two ranks of oxygens on the [1010] ice prism plane in the <0001> direction, giving high ice-binding affinity and specificity. This binding site, substantiated by the structures and properties of several ice-binding site mutants, suggests that the AFP occupies a niche in the ice surface in which it covers the basal plane while binding to the prism face.

==About this Structure==

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[[Category: thermal hysteresis protein]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-Antifreeze proteins (AFPs) have the unique ability to adsorb to ice and, inhibit its growth. Many organisms ranging from fish to bacteria use AFPs, to retard freezing or lessen the damage incurred upon freezing and, thawing. The ice-binding mechanism of the long linear alpha-helical type I, AFPs has been attributed to their regularly spaced polar residues matching, the ice lattice along a pyramidal plane. In contrast, it is not known how, globular antifreeze proteins such as type III AFP that lack repeating, ice-binding residues bind to ice. Here we report the 1.25 A crystal, structure of recombinant type III AFP (QAE isoform) from eel pout, (Macrozoarces americanus), which reveals a remarkably flat amphipathic, ice-binding site where five hydrogen-bonding atoms match two ranks of, oxygens on the [1010] ice prism plane in the &lt;0001&gt; direction, giving high, ice-binding affinity and specificity. This binding site, substantiated by, the structures and properties of several ice-binding site mutants, suggests that the AFP occupies a niche in the ice surface in which it, covers the basal plane while binding to the prism face.
+Antifreeze proteins (AFPs) have the unique ability to adsorb to ice and inhibit its growth. Many organisms ranging from fish to bacteria use AFPs to retard freezing or lessen the damage incurred upon freezing and thawing. The ice-binding mechanism of the long linear alpha-helical type I AFPs has been attributed to their regularly spaced polar residues matching the ice lattice along a pyramidal plane. In contrast, it is not known how globular antifreeze proteins such as type III AFP that lack repeating ice-binding residues bind to ice. Here we report the 1.25 A crystal structure of recombinant type III AFP (QAE isoform) from eel pout (Macrozoarces americanus), which reveals a remarkably flat amphipathic ice-binding site where five hydrogen-bonding atoms match two ranks of oxygens on the [1010] ice prism plane in the &lt;0001&gt; direction, giving high ice-binding affinity and specificity. This binding site, substantiated by the structures and properties of several ice-binding site mutants, suggests that the AFP occupies a niche in the ice surface in which it covers the basal plane while binding to the prism face.
 ==About this Structure==
@@ Line 23: / Line 23: @@
 [[Category: thermal hysteresis protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:52:05 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:10:30 2008''