Structure of the alpha-amylase inhibitor tendamistat at 0.93 A.

IF 2.2 4区生物学 Acta Crystallographica Section D: Biological Crystallography Pub Date : 2004-01-15 DOI:10.2210/PDB1OK0/PDB

V. König, L. Vértesy, T. Schneider

引用次数: 2

Abstract

The crystal structure of the proteinaceous alpha-amylase inhibitor tendamistat has been determined at 100 K to a resolution of 0.93 A. The final R factor for all reflections with F > 4sigma(F) is 9.26%. The mean coordinate error for fully occupied protein atoms as derived from full-matrix inversion is 0.018 A. An extended network of multiple discrete conformations has been identified on the side of tendamistat that binds to the target molecule. Most notably, residue Tyr15, which interacts with the glycine-rich loop characteristic of mammalian amylases, and a cluster of amino-acid side chains surrounding it are found in two well defined conformations. The flexibility observed in this crystal structure together with information about residues fixed by lattice contacts in the crystal but found to be mobile in a previous NMR study supports a model in which most of the residues involved in binding are not fixed in the free form of the inhibitor, suggesting an induced-fit type of binding.

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α -淀粉酶抑制剂tendamistat在0.93 A时的结构。

蛋白型α -淀粉酶抑制剂tendamistat的晶体结构在100 K下测定，分辨率为0.93 a。所有F > 4 σ (F)反射的最终R因子为9.26%。由全矩阵反演得到的完全占据的蛋白质原子的平均坐标误差为0.018 A。在与靶分子结合的tendamistat的一侧已经确定了多个离散构象的扩展网络。最值得注意的是，残基Tyr15与哺乳动物淀粉酶的富含甘氨酸的环相互作用，其周围有一簇氨基酸侧链，具有两种明确的构象。在这种晶体结构中观察到的柔韧性，以及晶体中晶格接触固定的残基信息，但在之前的核磁共振研究中发现残基是可移动的，这支持了一个模型，在这个模型中，参与结合的大多数残基并不固定在抑制剂的自由形式中，这表明了一种诱导配合类型的结合。

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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来源期刊

Acta Crystallographica Section D: Biological Crystallography 生物-晶体学

自引率

13.60%

发文量

审稿时长

3 months

期刊介绍： Acta Crystallographica Section D welcomes the submission of articles covering any aspect of structural biology, with a particular emphasis on the structures of biological macromolecules or the methods used to determine them. Reports on new structures of biological importance may address the smallest macromolecules to the largest complex molecular machines. These structures may have been determined using any structural biology technique including crystallography, NMR, cryoEM and/or other techniques. The key criterion is that such articles must present significant new insights into biological, chemical or medical sciences. The inclusion of complementary data that support the conclusions drawn from the structural studies (such as binding studies, mass spectrometry, enzyme assays, or analysis of mutants or other modified forms of biological macromolecule) is encouraged. Methods articles may include new approaches to any aspect of biological structure determination or structure analysis but will only be accepted where they focus on new methods that are demonstrated to be of general applicability and importance to structural biology. Articles describing particularly difficult problems in structural biology are also welcomed, if the analysis would provide useful insights to others facing similar problems.

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