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首页> 外文期刊>Journal of Molecular Biology >Crystal structure of unligated guanylate kinase from yeast revealsGMP-induced conformational changes
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Crystal structure of unligated guanylate kinase from yeast revealsGMP-induced conformational changes

机译：来自酵母的未连接鸟苷酸激酶的晶体结构揭示了GMP诱导的构象变化

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The crystal structure of guanylate kinase (GK) from yeast (Saccharomyces cerevisiae) with a non-acetylated N terminus has been determined in its unligated form (apo-GK) as well as in complex with GMP (GK CMF). The structure of apo-GK was solved with multiwavelength anomalous diffraction data and refined to an X-factor of 0.164 (R-free = 0.199) at 2.3 Angstrom resolution. The structure of GK (.) GMP was determined using the crystal structure of GK with an acetylated N terminus as the search model and refined to an R-factor of 0.156 (R-free = 0.245) at 1.9 Angstrom. GK belongs to the family of nucleoside monophosphate (NMP) kinases and catalyzes the reversible phosphoryl transfer from ATP to GMP. Like other NMP kinases, GK consists of three dynamic domains: the CORE, LID, and NMP-binding domains. Dramatic movements of the GMP-binding domain and smaller but significant movements of the LID domain have been revealed by comparing the structures of apo-CK and GK (.) GMP. apo-GK has a much more open conformation than the GK GMP complex. Systematic analysis of the domain movements using the program DynDom shows that the large movements of the GMP-binding domain involve a rotation around an effective hinge axis approximately parallel with helix 3, which connects the GMP-binding and CORE domains. The C-terminal portion of helix 3, which connects to the CORE domain, has strikingly higher temperature factors in GK (.) GMP than in apo-CK, indicating that these residues become more mobile upon CMP binding. The results suggest that helix 3 plays an important role in domain movement. Unlike the GMP-binding domain, which moves toward the active center of the enzyme upon GMP binding, the LID domain moves away from the active center and makes the presumed ATP-binding site more open. Therefore, the LID domain movement may facilitate the binding of MgATP. The structure of the recombinant GK (.) CMP complex superimposes very well with that of the native GK (.) GMP complex, indicating that N-terminal acetylation does not have significant impact on the three-dimensional structure of GK.
机译：已确定未连接形式（apo-GK）以及与GMP的复合物（GK CMF）的带有未乙酰化N末端的酵母（Saccharomyces cerevisiae）的鸟苷酸激酶（GK）的晶体结构。用多波长异常衍射数据解析了apo-GK的结构，并在2.3埃分辨率下将其精制为X因子0.164（无R = 0.199）。使用具有乙酰化N末端的GK晶体结构作为搜索模型来确定GK（。）GMP的结构，并在1.9埃时将其精制到R因子0.156（无R = 0.245）。 GK属于核苷单磷酸（NMP）激酶家族，催化从ATP到GMP的可逆磷酸转移。像其他NMP激酶一样，GK由三个动态域组成：CORE，LID和NMP结合域。通过比较apo-CK和GK（。）GMP的结构，揭示了GMP结合域的剧烈运动和LID域的较小但重要的运动。载脂蛋白GK比GK GMP复杂得多。使用程序DynDom对域运动的系统分析表明，GMP绑定域的大运动涉及围绕有效铰链轴的旋转，该轴近似平行于连接GMP绑定域和CORE域的螺旋3。螺旋3的C端部分（与CORE域相连）在GK（。）GMP中的温度因子比在apo-CK中高得多，这表明这些残基在CMP结合后变得更具流动性。结果表明，螺旋3在域运动中起重要作用。与GMP结合结构域（在GMP结合后会移向酶的活性中心）不同，LID域从活性中心移开，使推测的ATP结合位点更加开放。因此，LID结构域的移动可能有助于MgATP的绑定。重组GK（。）CMP复合物的结构与天然GK（。）GMP复合物的结构很好地重叠，表明N末端乙酰化对GK的三维结构没有重大影响。

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