3ZQQ

Crystal structure of the full-length small terminase from a SPP1-like bacteriophage

3ZQQ の概要

• エントリーDOI: 10.2210/pdb3zqq/pdb
• 関連するPDBエントリー: 3ZQM 3ZQN 3ZQO 3ZQP
• 分子名称: TERMINASE SMALL SUBUNIT (1 entity in total)
• 機能のキーワード: dna-binding protein, dna packaging, dna binding protein
• 由来する生物種: BACILLUS PHAGE SF6
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 54208.73

構造登録者

Buttner, C.R.,Chechik, M.,Ortiz-Lombardia, M.,Smits, C.,Chechik, V.,Jeschke, G.,Dykeman, E.,Benini, S.,Alonso, J.C.,Antson, A.A. (登録日: 2011-06-10, 公開日: 2011-12-28, 最終更新日: 2023-12-20)

主引用文献

Buttner, C.R.,Chechik, M.,Ortiz-Lombardia, M.,Smits, C.,Ebong, I.O.,Chechik, V.,Jeschke, G.,Dykeman, E.,Benini, S.,Robinson, C.V.,Alonso, J.C.,Antson, A.A.
Structural Basis for DNA Recognition and Loading Into a Viral Packaging Motor.
Proc.Natl.Acad.Sci.USA, 109:811-, 2012

PubMed Abstract: Genome packaging into preformed viral procapsids is driven by powerful molecular motors. The small terminase protein is essential for the initial recognition of viral DNA and regulates the motor's ATPase and nuclease activities during DNA translocation. The crystal structure of a full-length small terminase protein from the Siphoviridae bacteriophage SF6, comprising the N-terminal DNA binding, the oligomerization core, and the C-terminal β-barrel domains, reveals a nine-subunit circular assembly in which the DNA-binding domains are arranged around the oligomerization core in a highly flexible manner. Mass spectrometry analysis and four further crystal structures show that, although the full-length protein exclusively forms nine-subunit assemblies, protein constructs missing the C-terminal β-barrel form both nine-subunit and ten-subunit assemblies, indicating the importance of the C terminus for defining the oligomeric state. The mechanism by which a ring-shaped small terminase oligomer binds viral DNA has not previously been elucidated. Here, we probed binding in vitro by using EPR and surface plasmon resonance experiments, which indicated that interaction with DNA is mediated exclusively by the DNA-binding domains and suggested a nucleosome-like model in which DNA binds around the outside of the protein oligomer.

PubMed: 22207627
DOI: 10.1073/PNAS.1110270109

実験手法

X-RAY DIFFRACTION (4 Å)