2O0J

T4 gp17 ATPase domain mutant complexed with ADP

2O0J の概要

• エントリーDOI: 10.2210/pdb2o0j/pdb
• 関連するPDBエントリー: 2O0H 2O0K
• 分子名称: DNA packaging protein Gp17, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• 機能のキーワード: nucleotide-binding fold, hydrolase
• 由来する生物種: Enterobacteria phage T4
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 44652.30

構造登録者

Sun, S.,Rossmann, M.G. (登録日: 2006-11-27, 公開日: 2007-04-03, 最終更新日: 2023-08-30)

主引用文献

Sun, S.,Kondabagil, K.,Gentz, P.M.,Rossmann, M.G.,Rao, V.B.
The Structure of the ATPase that Powers DNA Packaging into Bacteriophage T4 Procapsids
MOL.CELL, 25:943-949, 2007

PubMed Abstract: Packaging the viral genome into empty procapsids, an essential event in the life cycle of tailed bacteriophages and some eukaryotic viruses, is a process that shares features with chromosome assembly. Most viral procapsids possess a special vertex containing a dodecameric portal protein that is used for entry and exit of the viral genome. The portal and an ATPase are parts of the genome-packaging machine. The ATPase is required to provide energy for translocation and compaction of the negative charges on the genomic DNA. Here we report the atomic structure of the ATPase component in a phage DNA-packaging machine. The bacteriophage T4 ATPase has the greatest similarity to monomeric helicases, suggesting that the genome is translocated by an inchworm mechanism. The similarity of the packaging machines in the double-stranded DNA (dsDNA) bacteriophage T4 and dsRNA bacteriophage varphi12 is consistent with the evolution of many virions from a common ancestor.

PubMed: 17386269
DOI: 10.1016/j.molcel.2007.02.013

実験手法

X-RAY DIFFRACTION (1.8 Å)