5HD9

Crystal Structure of the N-terminal domain of the DNA packaging ATPase from bacteriophage phi29

5HD9 の概要

• エントリーDOI: 10.2210/pdb5hd9/pdb
• 分子名称: Encapsidation protein (2 entities in total)
• 機能のキーワード: asce fold, viral protein
• 由来する生物種: Bacillus phage phi29
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22854.63

構造登録者

Morais, M.C.,Mao, H.,Reyes-Aldrete, E. (登録日: 2016-01-05, 公開日: 2016-03-09, 最終更新日: 2024-10-16)

主引用文献

Mao, H.,Saha, M.,Reyes-Aldrete, E.,Sherman, M.B.,Woodson, M.,Atz, R.,Grimes, S.,Jardine, P.J.,Morais, M.C.
Structural and Molecular Basis for Coordination in a Viral DNA Packaging Motor.
Cell Rep, 14:2017-2029, 2016

PubMed Abstract: Ring NTPases are a class of ubiquitous molecular motors involved in basic biological partitioning processes. dsDNA viruses encode ring ATPases that translocate their genomes to near-crystalline densities within pre-assembled viral capsids. Here, X-ray crystallography, cryoEM, and biochemical analyses of the dsDNA packaging motor in bacteriophage phi29 show how individual subunits are arranged in a pentameric ATPase ring and suggest how their activities are coordinated to translocate dsDNA. The resulting pseudo-atomic structure of the motor and accompanying functional analyses show how ATP is bound in the ATPase active site; identify two DNA contacts, including a potential DNA translocating loop; demonstrate that a trans-acting arginine finger is involved in coordinating hydrolysis around the ring; and suggest a functional coupling between the arginine finger and the DNA translocating loop. The ability to visualize the motor in action illuminates how the different motor components interact with each other and with their DNA substrate.

PubMed: 26904950
DOI: 10.1016/j.celrep.2016.01.058

実験手法

X-RAY DIFFRACTION (1.941 Å)