Isomerization mechanism of aspartate to isoaspartate implied by structures of Ustilago sphaerogena ribonuclease U2 complexed with adenosine 3'-monophosphate.

Noguchi S

首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Isomerization mechanism of aspartate to isoaspartate implied by structures of Ustilago sphaerogena ribonuclease U2 complexed with adenosine 3'-monophosphate.

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Isomerization mechanism of aspartate to isoaspartate implied by structures of Ustilago sphaerogena ribonuclease U2 complexed with adenosine 3'-monophosphate.

机译：天冬氨酸的异构化机理isoaspartate隐含黑粉菌属的结构sphaerogena核糖核酸酶U2包裹着一磷酸腺苷3”。

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Aspartates in proteins are isomerized non-enzymatically to isoaspartate via succinimide in vitro and in vivo. In order to elucidate the mechanism of isoaspartate formation within the Asp45-Glu46 sequence of Ustilago sphaerogena ribonuclease U2 based on three-dimensional structure, crystal structures of ribonuclease U2 complexed with adenosine 3'-monophosphate have been solved at 0.96 and 0.99 A resolution. The crystal structures revealed that the C(gamma) atom of Asp45 is located just beside the main-chain N atom of Glu46 and that the conformation which is suitable for succinimide formation is stabilized by a hydrogen-bond network mediated by water molecules 190, 219 and 220. These water molecules are suggested to promote the formation of isoaspartate via succinimide: in the succinimide-formation reaction water 219 receives a proton from the N atom of Glu46 as a general base and waters 190 and 220 stabilize the tetrahedral intermediate, and in the succinimide-hydrolysis reaction water 219 provides a proton for the N atom of Glu46 as a general acid. The purine-base recognition scheme of ribonuclease U2 is also discussed.

机译：天冬氨酸蛋白质异构化的non-enzymatically isoaspartate通过琥珀酰亚胺在体外和体内。isoaspartate形成的机制Asp45-Glu46序列的黑粉菌属sphaerogena基于三维的核糖核酸酶U2核糖核酸酶的结构、晶体结构U2包裹着的一磷酸腺苷3解决了在0.96和0.99的决议。晶体结构表明,C(γ)原子的Asp45坐落的旁边主链的N原子Glu46,适用于琥珀酰亚胺的构象形成稳定的形成氢键网络由水分子190年、219年和220. 促进isoaspartate通过的形成琥珀酰亚胺:succinimide-formation反应水从N 219接收一个质子原子的Glu46一般基础和水域190和220年稳定的四面体中间,水和succinimide-hydrolysis反应219提供了一个为Glu46 N原子的质子一般的酸。核糖核酸酶U2方案也进行了讨论。

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《Acta crystallographica.Section D. Biological crystallography》 |2010年第7期|843-849|共7页
作者
Noguchi S;
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作者单位

Graduate School of Pharmaceutical Sciences, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.;

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正文语种英语
中图分类化学;
关键词
succinimide; CONNECTED NETWORKS; crystal structureAspartateCOPPER ALLOY NO 210AdenosineIsoaspartateAtomsUstilagoAspartic Acidhydrogen ions;

机译：琥珀酰亚胺,连接网络;晶体structureAspartateCOPPER合金没有;

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Isomerization mechanism of aspartate to isoaspartate implied by structures of Ustilago sphaerogena ribonuclease U2 complexed with adenosine 3'-monophosphate.

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