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首页> 外文期刊>Journal of Molecular Biology >The crystal structure of protein MJ1225 from Methanocaldococcus jannaschii shows strong conservation of key structural features seen in the eukaryal gamma-AMPK.
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The crystal structure of protein MJ1225 from Methanocaldococcus jannaschii shows strong conservation of key structural features seen in the eukaryal gamma-AMPK.

机译：詹氏甲烷球菌的MJ1225蛋白的晶体结构显示出在真核γ-AMPK中看到的关键结构特征的强烈保守性。

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摘要

In mammals, 5'-AMP-activated protein kinase (AMPK) is a heterotrimeric protein composed of a catalytic serine/threonine kinase subunit (alpha) and two regulatory subunits (beta and gamma). The gamma-subunit senses the intracellular energy status by competitively binding AMP and ATP and is thought to be responsible for allosteric regulation of the whole complex. We describe herein the crystal structure of protein MJ1225 from Methanocaldococcus jannaschii complexed to AMP, ADP, and ATP. Our data provide evidence of a strong conservation of the key functional features seen in the gamma-subunit of the eukaryotic AMPK, and more importantly, it reveals a novel AMP binding site, herein denoted as site E, which had not been previously described in cystathionine beta-synthase domains so far. Site E is located in a small cavity existing between the alpha-helices structurally equivalent to those disrupting the internal symmetry of each Bateman domain in gamma-AMPKs and shows striking similarities with a symmetry-related crevice of the mammalian enzyme that hosts the pathological mutation N488I.
机译：在哺乳动物中，5'-AMP激活的蛋白激酶（AMPK）是由催化丝氨酸/苏氨酸激酶亚基（alpha）和两个调节性亚基（beta和gamma）组成的异三聚体蛋白。 γ亚基通过竞争性结合AMP和ATP来感知细胞内能量状态，并被认为负责整个复合物的变构调节。我们在本文中描述了来自詹氏甲烷球菌的蛋白MJ1225的晶体结构，与AMP，ADP和ATP络合。我们的数据提供了在真核AMPK的γ亚基中看到的关键功能特征的强大保守性的证据，更重要的是，它揭示了一个新的AMP结合位点，在此表示为位点E，以前在胱硫醚中没有描述过到目前为止，β-合酶结构域。位点E位于一个小腔中，该小腔在结构上等同于破坏γ-AMPK中每个贝特曼域的内部对称性的α螺旋，并且与宿主病理突变N488I的哺乳动物酶的对称相关缝隙表现出惊人的相似性。

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