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4MXE

Human ESCO1 (Eco1/Ctf7 ortholog), acetyltransferase domain in complex with acetyl-CoA

4MXE の概要
エントリーDOI10.2210/pdb4mxe/pdb
分子名称N-acetyltransferase ESCO1, ACETYL COENZYME *A (3 entities in total)
機能のキーワードstructural genomics, structural genomics consortium, sgc, gcn5-related n-acetyltransferase fold, acetyltransferase, nucleus, transferase
由来する生物種Homo sapiens (human)
細胞内の位置Nucleus : Q5FWF5
タンパク質・核酸の鎖数2
化学式量合計49616.83
構造登録者
主引用文献Kouznetsova, E.,Kanno, T.,Karlberg, T.,Thorsell, A.G.,Wisniewska, M.,Kursula, P.,Sjogren, C.,Schuler, H.
Sister Chromatid Cohesion Establishment Factor ESCO1 Operates by Substrate-Assisted Catalysis.
Structure, 24:789-796, 2016
Cited by
PubMed Abstract: Sister chromatid cohesion, formed by the cohesin protein complex, is essential for chromosome segregation. In order for cohesion to be established, the cohesin subunit SMC3 needs to be acetylated by a homolog of the ESCO1/Eco1 acetyltransferases, the enzymatic mechanism of which has remained unknown. Here we report the crystal structure of the ESCO1 acetyltransferase domain in complex with acetyl-coenzyme A, and show by SAXS that ESCO1 is a dimer in solution. The structure reveals an active site that lacks a potential catalytic base side chain. However, mutation of glutamate 789, a surface residue that is close to the automodification target lysine 803, strongly reduces autoacetylation of ESCO1. Moreover, budding yeast Smc3 mutated at the conserved residue D114, adjacent to the cohesion-activating acetylation site K112,K113, cannot be acetylated in vivo. This indicates that ESCO1 controls cohesion through substrate-assisted catalysis. Thus, this study discloses a key mechanism for cohesion establishment.
PubMed: 27112597
DOI: 10.1016/j.str.2016.03.021
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.6 Å)
構造検証レポート
Validation report summary of 4mxe
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2026-02-04に公開中

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