4MXE
Human ESCO1 (Eco1/Ctf7 ortholog), acetyltransferase domain in complex with acetyl-CoA
4MXE の概要
| エントリーDOI | 10.2210/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 | Karlberg, T.,Wisniewska, M.,Thorsell, A.G.,Kouznetsova, E.,Arrowsmith, C.H.,Berglund, H.,Bountra, C.,Collins, R.,Edwards, A.M.,Flodin, S.,Flores, A.,Graslund, S.,Hammarstrom, M.,Johansson, I.,Kallas, A.,Kraulis, P.,Kotenyova, T.,Moche, M.,Nielsen, T.K.,Nordlund, P.,Nyman, T.,Persson, C.,Schutz, P.,Svensson, L.,Tresaugues, L.,Van Den Berg, S.,Wahlberg, E.,Weigelt, J.,Welin, M.,Schuler, H.,Structural Genomics Consortium (SGC) (登録日: 2013-09-26, 公開日: 2015-04-08, 最終更新日: 2024-11-06) |
| 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: 27112597DOI: 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) |
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