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4LRK

Bacterial Effector NleH2 Kinase Domain

4LRK の概要
エントリーDOI10.2210/pdb4lrk/pdb
関連するPDBエントリー4LRJ
分子名称Effector NleH2 (2 entities in total)
機能のキーワードstructural genomics, montreal-kingston bacterial structural genomics initiative, bsgi, kinase fold, bacterial effector kinase, transferase
由来する生物種Escherichia coli
タンパク質・核酸の鎖数4
化学式量合計74791.59
構造登録者
Cygler, M.,Grishin, A.M.,Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (登録日: 2013-07-19, 公開日: 2014-01-22, 最終更新日: 2024-02-28)
主引用文献Grishin, A.M.,Cherney, M.,Anderson, D.H.,Phanse, S.,Babu, M.,Cygler, M.
NleH defines a new family of bacterial effector kinases.
Structure, 22:250-259, 2014
Cited by
PubMed Abstract: Upon host cell infection, pathogenic Escherichia coli hijacks host cellular processes with the help of 20-60 secreted effector proteins that subvert cellular processes to create an environment conducive to bacterial survival. The NleH effector kinases manipulate the NF-κB pathway and prevent apoptosis. They show low sequence similarity to human regulatory kinases and contain two domains, the N-terminal, likely intrinsically unfolded, and a C-terminal kinase-like domain. We show that these effectors autophosphorylate on sites located predominantly in the N-terminal segment. The kinase domain displays a minimal kinase fold, but lacks an activation loop and the GHI subdomain. Nevertheless, all catalytically important residues are conserved. ATP binding proceeds with minimal structural rearrangements. The NleH structure is the first for the bacterial effector kinases family. NleHs and their homologous effector kinases form a new kinase family within the cluster of eukaryotic-like kinases that includes also Rio, Bud32, and KdoK families.
PubMed: 24373767
DOI: 10.1016/j.str.2013.11.006
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.274 Å)
構造検証レポート
Validation report summary of 4lrk
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2025-04-09に公開中

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