Cold survival in freeze-intolerant insects: the structure and function of beta-helical antifreeze proteins.

Steffen P Graether, Brian D Sykes
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引用次数: 123

Abstract

Antifreeze proteins (AFPs) designate a class of proteins that are able to bind to and inhibit the growth of macromolecular ice. These proteins have been characterized from a variety of organisms. Recently, the structures of AFPs from the spruce budworm (Choristoneura fumiferana) and the yellow mealworm (Tenebrio molitor) have been determined by NMR and X-ray crystallography. Despite nonhomologous sequences, both proteins were shown to consist of beta-helices. We review the structures and dynamics data of these two insect AFPs to bring insight into the structure-function relationship and explore their beta-helical architecture. For the spruce budworm protein, the fold is a left-handed beta-helix with 15 residues per coil. The Tenebrio molitor protein consists of a right-handed beta-helix with 12 residues per coil. Mutagenesis and structural studies show that the insect AFPs present a highly rigid array of threonine residues and bound water molecules that can effectively mimic the ice lattice. 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.

抗冻昆虫的低温存活:β -螺旋抗冻蛋白的结构和功能。
抗冻蛋白(AFPs)是一类能够结合并抑制大分子冰生长的蛋白质。这些蛋白质已经从各种生物体中被鉴定出来。近年来,利用核磁共振和x射线晶体学技术对云杉budworm (Choristoneura fumiferana)和黄粉虫(Tenebrio molitor)的AFPs结构进行了研究。尽管非同源序列,这两种蛋白质都显示由β -螺旋组成。本文回顾了这两种昆虫蛋白的结构和动力学数据,以进一步了解它们的结构-功能关系,并探索它们的β -螺旋结构。对于云杉budworm蛋白,折叠是一个左旋β -螺旋,每圈有15个残基。tenbrio molitor蛋白由一个右旋β -螺旋组成,每个螺旋有12个残基。诱变和结构研究表明,昆虫afp呈现出高度刚性的苏氨酸残基和结合水分子阵列,可以有效地模拟冰格。通过比较新确定的黑麦草和胡萝卜AFP序列,模型表明它们也可能由β -螺旋组成,并表明β -螺旋可能在非鱼类生物中用作AFP结构基序。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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