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1IKA

STRUCTURE OF ISOCITRATE DEHYDROGENASE WITH ALPHA-KETOGLUTARATE AT 2.7 ANGSTROMS RESOLUTION: CONFORMATIONAL CHANGES INDUCED BY DECARBOXYLATION OF ISOCITRATE

1IKA の概要
エントリーDOI10.2210/pdb1ika/pdb
分子名称ISOCITRATE DEHYDROGENASE, CALCIUM ION, 2-OXOGLUTARIC ACID (3 entities in total)
機能のキーワードoxidoreductase(nad(a)-choh(d))
由来する生物種Escherichia coli
タンパク質・核酸の鎖数1
化学式量合計45995.74
構造登録者
Stoddard, B.L.,Koshland Junior, D.E. (登録日: 1993-06-15, 公開日: 1994-07-31, 最終更新日: 2024-02-07)
主引用文献Stoddard, B.L.,Koshland Jr., D.E.
Structure of isocitrate dehydrogenase with alpha-ketoglutarate at 2.7-A resolution: conformational changes induced by decarboxylation of isocitrate.
Biochemistry, 32:9317-9322, 1993
Cited by
PubMed Abstract: The structure of the isocitrate dehydrogenase (IDH) complex with bound alpha-ketoglutarate, Ca2+, and NADPH was solved at 2.7-A resolution. The alpha-ketoglutarate binds in the active site at the same position and orientation as isocitrate, with a difference between the two bound molecules of about 0.8 A. The Ca2+ metal is coordinated by alpha-ketoglutarate, three conserved aspartate residues, and a pair of water molecules. The largest motion in the active site relative to the isocitrate enzyme complex is observed for tyrosine 160, which originally forms a hydrogen bond to the labile carboxyl group of isocitrate and moves to form a new hydrogen bond to Asp 307 in the complex with alpha-ketoglutarate. This triggers a number of significant movements among several short loops and adjoining secondary structural elements in the enzyme, most of which participate in dimer stabilization and formation of the active-site cleft. These rearrangements are similar to the ligand-binding-induced movements observed in globins and insulin and serve as a model for an enzymatic mechanism which involves local shifts of secondary structural elements during turnover, rather than large-scale domain closures or loop transitions induced by substrate binding such as those observed in hexokinase or triosephosphate isomerase.
PubMed: 8369301
DOI: 10.1021/bi00087a009
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.7 Å)
構造検証レポート
Validation report summary of 1ika
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-04-02に公開中

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