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首页> 外文期刊>Biological chemistry >The structure of the nucleotide-binding site of kinesin.
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The structure of the nucleotide-binding site of kinesin.

机译：Kinesin核苷酸结合位点的结构。

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Kinesin is a microtubule-based motor protein responsible for anterograde transport of vesicles and organelles in nerve axons and other cell types. The energy necessary for this transport is derived from the hydrolysis of ATP which is thought to induce conformational changes in the protein. We have solved the X-ray crystal structures of rat brain kinesin in three conditions intended to mimic different nucleotide states: (1) with ADP bound to the nucleotide-binding site, (2) with bound ADP in the presence of AIF(-)4, and (3) with ADP hydrolyzed to AMP by apyrase. In contrast to analogous cases observed in GTP-binding proteins or the muscle motor myosin, the structure of kinesin remained nearly unchanged. This highlights the stability of kinesin's ADP state in the absence of microtubules. Surprisingly, even after hydrolysis of ADP to AMP by apyrase a strong density peak remains at the position of the beta-phosphate which is compatible either with a phosphate or a sulfate from the solvent and appears to stabilize the nucleotide-binding pocket through several hydrogen bonds.
机译：Kinesin是一种基于微管的电动蛋白，负责神经轴突和其他细胞类型中的囊泡和细胞器的前瓣传输。该转运所需的能量来自ATP的水解，该方法被认为诱导蛋白质的构象变化。我们在三种条件下解决了大鼠脑动素的X射线晶体结构，用于模拟不同核苷酸状态：（1）与核苷酸结合位点结合的ADP，在AIF（ - ）存在下用结合的ADP结合4，和（3）ADP通过亚紫外酶水解成AMP。与GTP结合蛋白或肌肉电机肌蛋白中观察到的类似案例相反，Kinesin的结构几乎保持不变。这突出了在没有微管的情况下kinesin的ADP状态的稳定性。令人惊讶的是，即使通过紫外酶水解ADP到AMP，强密度峰保持在β-磷酸盐的位置，其与磷酸盐或来自溶剂的硫酸盐相容，并且似乎通过几个氢键稳定核苷酸结合口袋。

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