2ICT

Crystal structure of the bacterial antitoxin HigA from Escherichia coli at pH 8.5. Northeast Structural Genomics TARGET ER390.

2ICT の概要

• エントリーDOI: 10.2210/pdb2ict/pdb
• 関連するPDBエントリー: 2ICP
• 分子名称: antitoxin higa (2 entities in total)
• 機能のキーワード: helix-turn-helix, structural genomics, psi-2, protein structure initiative, northeast structural genomics consortium, nesg, dna binding protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10647.54

構造登録者

Arbing, M.A.,Abashidze, M.,Hurley, J.M.,Zhao, L.,Janjua, H.,Cunningham, K.,Ma, L.C.,Xiao, R.,Liu, J.,Baran, M.C.,Acton, T.B.,Rost, B.,Inouye, M.,Woychik, N.A.,Montelione, G.T.,Hunt, J.F.,Northeast Structural Genomics Consortium (NESG) (登録日: 2006-09-13, 公開日: 2006-09-26, 最終更新日: 2017-10-18)

主引用文献

Arbing, M.A.,Handelman, S.K.,Kuzin, A.P.,Verdon, G.,Wang, C.,Su, M.,Rothenbacher, F.P.,Abashidze, M.,Liu, M.,Hurley, J.M.,Xiao, R.,Acton, T.,Inouye, M.,Montelione, G.T.,Woychik, N.A.,Hunt, J.F.
Crystal Structures of Phd-Doc, HigA, and YeeU Establish Multiple Evolutionary Links between Microbial Growth-Regulating Toxin-Antitoxin Systems.
Structure, 18:996-1010, 2010

PubMed Abstract: Bacterial toxin-antitoxin (TA) systems serve a variety of physiological functions including regulation of cell growth and maintenance of foreign genetic elements. Sequence analyses suggest that TA families are linked by complex evolutionary relationships reflecting likely swapping of functional domains between different TA families. Our crystal structures of Phd-Doc from bacteriophage P1, the HigA antitoxin from Escherichia coli CFT073, and YeeU of the YeeUWV systems from E. coli K12 and Shigella flexneri confirm this inference and reveal additional, unanticipated structural relationships. The growth-regulating Doc toxin exhibits structural similarity to secreted virulence factors that are toxic for eukaryotic target cells. The Phd antitoxin possesses the same fold as both the YefM and NE2111 antitoxins that inhibit structurally unrelated toxins. YeeU, which has an antitoxin-like activity that represses toxin expression, is structurally similar to the ribosome-interacting toxins YoeB and RelE. These observations suggest extensive functional exchanges have occurred between TA systems during bacterial evolution.

PubMed: 20696400
DOI: 10.1016/j.str.2010.04.018

実験手法

X-RAY DIFFRACTION (1.63 Å)