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4KVA

GTPase domain of Septin 10 from Schistosoma mansoni in complex with GTP

4KVA の概要
エントリーDOI10.2210/pdb4kva/pdb
関連するPDBエントリー4KV9
分子名称Septin, GUANOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
機能のキーワードsmall gtpase, cytoskeleton component, hydrolase
由来する生物種Schistosoma mansoni (Blood fluke)
タンパク質・核酸の鎖数2
化学式量合計97407.35
構造登録者
Zeraik, A.E.,Pereira, H.M.,Santos, Y.V.,Brandao-Neto, J.,Garratt, R.C.,Araujo, A.P.U.,Demarco, R. (登録日: 2013-05-22, 公開日: 2014-02-05, 最終更新日: 2024-04-03)
主引用文献Zeraik, A.E.,Pereira, H.M.,Santos, Y.V.,Brandao-Neto, J.,Spoerner, M.,Santos, M.S.,Colnago, L.A.,Garratt, R.C.,Araujo, A.P.,Demarco, R.
Crystal Structure of a Schistosoma mansoni Septin Reveals the Phenomenon of Strand Slippage in Septins Dependent on the Nature of the Bound Nucleotide.
J.Biol.Chem., 289:7799-7811, 2014
Cited by
PubMed Abstract: Septins are filament-forming GTP-binding proteins involved in important cellular events, such as cytokinesis, barrier formation, and membrane remodeling. Here, we present two crystal structures of the GTPase domain of a Schistosoma mansoni septin (SmSEPT10), one bound to GDP and the other to GTP. The structures have been solved at an unprecedented resolution for septins (1.93 and 2.1 Å, respectively), which has allowed for unambiguous structural assignment of regions previously poorly defined. Consequently, we provide a reliable model for functional interpretation and a solid foundation for future structural studies. Upon comparing the two complexes, we observe for the first time the phenomenon of a strand slippage in septins. Such slippage generates a front-back communication mechanism between the G and NC interfaces. These data provide a novel mechanistic framework for the influence of nucleotide binding to the GTPase domain, opening new possibilities for the study of the dynamics of septin filaments.
PubMed: 24464615
DOI: 10.1074/jbc.M113.525352
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.14 Å)
構造検証レポート
Validation report summary of 4kva
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2024-11-06に公開中

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