4BIL

Threading model of the T7 large terminase within the gp8gp19 complex

4BIL の概要

• エントリーDOI: 10.2210/pdb4bil/pdb
• 関連するPDBエントリー: 4BIJ
• EMDBエントリー: 2355 2356
• 分子名称: DNA MATURASE B (1 entity in total)
• 機能のキーワード: hydrolase, packaging motor, connector, dna translocation, atpase.
• 由来する生物種: ENTEROBACTERIA PHAGE T7
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 269112.52

構造登録者

Dauden, M.I.,Martin-Benito, J.,Sanchez-Ferrero, J.C.,Pulido-Cid, M.,Valpuesta, J.M.,Carrascosa, J.L. (登録日: 2013-04-10, 公開日: 2013-05-08, 最終更新日: 2024-05-08)

主引用文献

Dauden, M.I.,Martin-Benito, J.,Sanchez-Ferrero, J.C.,Pulido-Cid, M.,Valpuesta, J.M.,Carrascosa, J.L.
Large Terminase Conformational Change Induced by Connector Binding in Bacteriophage T7
J.Biol.Chem., 288:16998-, 2013

PubMed Abstract: During bacteriophage morphogenesis DNA is translocated into a preformed prohead by the complex formed by the portal protein, or connector, plus the terminase, which are located at an especial prohead vertex. The terminase is a powerful motor that converts ATP hydrolysis into mechanical movement of the DNA. Here, we have determined the structure of the T7 large terminase by electron microscopy. The five terminase subunits assemble in a toroid that encloses a channel wide enough to accommodate dsDNA. The structure of the complete connector-terminase complex is also reported, revealing the coupling between the terminase and the connector forming a continuous channel. The structure of the terminase assembled into the complex showed a different conformation when compared with the isolated terminase pentamer. To understand in molecular terms the terminase morphological change, we generated the terminase atomic model based on the crystallographic structure of its phage T4 counterpart. The docking of the threaded model in both terminase conformations showed that the transition between the two states can be achieved by rigid body subunit rotation in the pentameric assembly. The existence of two terminase conformations and its possible relation to the sequential DNA translocation may shed light into the molecular bases of the packaging mechanism of bacteriophage T7.

PubMed: 23632014
DOI: 10.1074/JBC.M112.448951

実験手法

ELECTRON MICROSCOPY (29 Å)