1CJA
ACTIN-FRAGMIN KINASE, CATALYTIC DOMAIN FROM PHYSARUM POLYCEPHALUM
1CJA の概要
| エントリーDOI | 10.2210/pdb1cja/pdb |
| 分子名称 | PROTEIN (ACTIN-FRAGMIN KINASE), ADENOSINE MONOPHOSPHATE (2 entities in total) |
| 機能のキーワード | kinase, actin, transferase |
| 由来する生物種 | Physarum polycephalum |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 76893.57 |
| 構造登録者 | Steinbacher, S.,Hof, P.,Eichinger, L.,Schleicher, M.,Gettemans, J.,Vandekerckhove, J.,Huber, R.,Benz, J. (登録日: 1999-04-08, 公開日: 1999-06-18, 最終更新日: 2024-02-07) |
| 主引用文献 | Steinbacher, S.,Hof, P.,Eichinger, L.,Schleicher, M.,Gettemans, J.,Vandekerckhove, J.,Huber, R.,Benz, J. The crystal structure of the Physarum polycephalum actin-fragmin kinase: an atypical protein kinase with a specialized substrate-binding domain. EMBO J., 18:2923-2929, 1999 Cited by PubMed Abstract: Coordinated temporal and spatial regulation of the actin cytoskeleton is essential for diverse cellular processes such as cell division, cell motility and the formation and maintenance of specialized structures in differentiated cells. In plasmodia of Physarum polycephalum, the F-actin capping activity of the actin-fragmin complex is regulated by the phosphorylation of actin. This is mediated by a novel type of protein kinase with no sequence homology to eukaryotic-type protein kinases. Here we present the crystal structure of the catalytic domain of the first cloned actin kinase in complex with AMP at 2.9 A resolution. The three-dimensional fold reveals a catalytic module of approximately 160 residues, in common with the eukaryotic protein kinase superfamily, which harbours the nucleotide binding site and the catalytic apparatus in an inter-lobe cleft. Several kinases that share this catalytic module differ in the overall architecture of their substrate recognition domain. The actin-fragmin kinase has acquired a unique flat substrate recognition domain which is supposed to confer stringent substrate specificity. PubMed: 10357805DOI: 10.1093/emboj/18.11.2923 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.9 Å) |
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