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タイトル: Isomerization mechanism of aspartate to isoaspartate implied by structures of Ustilago sphaerogena ribonuclease U2 complexed with adenosine 3'-monophosphate
著者: Noguchi, Shuji
著者(別言語): 野口, 修治
キーワード: aspartate isomerization
発行日: 2010年7月
出版者: International Union of Crystallography
掲載誌情報: Acta crystallographica. Section D : Biological crystallography. Volume 66 Part 7, July 2010, pp. 843-849
抄録: 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 Å resolution. The crystal structures revealed that the C 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.
URI: http://hdl.handle.net/2261/37930
ISSN: 09074449
出現カテゴリ:1202010 学術雑誌論文
014 自然科学


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