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首页> 外文期刊>Journal of Molecular Biology >Crystal structures of a T4-lysozyme duplication-extension mutant demonstrate that the highly conserved beta-sheet region has low intrinsic folding propensity.
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Crystal structures of a T4-lysozyme duplication-extension mutant demonstrate that the highly conserved beta-sheet region has low intrinsic folding propensity.

机译：T4溶菌酶复制延伸突变体的晶体结构表明，高度保守的β-折叠区域具有较低的固有折叠倾向。

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摘要

Residues 24 to 35 of T4 lysozyme correspond to the second and third strands of a region of beta-sheet that is highly conserved in all known lysozyme and chitinase structures. To evaluate the intrinsic propensity of these amino acid residues to form a defined structure they were added at the C terminus of the native protein, together with a dipeptide linker. Two crystal structures of this active, mutant protein were obtained, to 1.9A and 2.3A resolution, respectively. Even though the crystal conditions are similar, the appended sequence adopts very different secondary structures. In one case it is weakly structured and appears to extend through the active-site cleft, perhaps in part adding an extra strand to the original beta-sheet. In the other crystal form the extension is largely alpha-helical. The formation of these alternative structures shows that the sequence does not have a strong intrinsic propensity to form a unique fold (either beta-sheet or otherwise). The results also suggest that structural conservation during evolution does not necessarily depend on sequence conservation or the conservation of folding propensity.
机译：T4溶菌酶的残基24至35对应于所有已知的溶菌酶和几丁质酶结构中高度保守的β-sheet区域的第二和第三条链。为了评估这些氨基酸残基形成限定结构的固有倾向，将它们与天然肽的C末端以及二肽接头一起添加。获得了该活性突变蛋白的两个晶体结构，分别达到了1.9A和2.3A的分辨率。即使晶体条件相似，附加序列也采用非常不同的二级结构。在一种情况下，它的结构较弱，似乎延伸穿过活动部位的裂缝，可能在一定程度上为原始β-折叠添加了一条额外的链。在另一种晶体形式中，延伸大部分是α-螺旋。这些替代结构的形成表明该序列不具有形成独特折叠（β-折叠或其他折叠）的强烈内在倾向。结果还表明，进化过程中的结构保守性不一定取决于序列保守性或折叠倾向的保守性。

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