2KN8

NMR structure of the C-terminal domain of pUL89

2KN8 の概要

• エントリーDOI: 10.2210/pdb2kn8/pdb
• NMR情報: BMRB: 16452
• 分子名称: DNA cleavage and packaging protein large subunit, UL89 (1 entity in total)
• 機能のキーワード: nhcmv, pul89, terminase, protein binding, dna binding protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7916.91

構造登録者

Couvreux, A.,Hantz, S.,Marquant, R.,Champier, G.,Alain, S.,Morellet, N.,Bouaziz, S. (登録日: 2009-08-18, 公開日: 2010-06-09, 最終更新日: 2024-05-01)

主引用文献

Couvreux, A.,Hantz, S.,Marquant, R.,Champier, G.,Alain, S.,Morellet, N.,Bouaziz, S.
Insight into the structure of the pUL89 C-terminal domain of the human cytomegalovirus terminase complex.
Proteins, 78:1520-1530, 2010

PubMed Abstract: In a previous study, we identified 12 conserved domains within pUL89, the small terminase subunit of the human cytomegalovirus. A latter study showed that the fragment pUL89(580-600) plays an important role in the formation of the terminase complex by interacting with the large terminase subunit pUL56. In this study, analysis was performed to solve the structure of pUL89(568-635) in 50% H2O/50% acetonitrile (v/v). We showed that pUL89(568-635) consists of four alpha helices, but we did not identify any tertiary structure. The fragment 580-600 formed an amphipathic alpha helix, which had a hydrophobic side highly conserved among herpesviral homologs of pUL89; this was not observed for its hydrophilic side. The modeling of pUL89(457-612) using the recognition fold method allowed us to position pUL89(580-600) within this domain. The theoretical structure highlighted three important features. First, we identified a metal-binding pocket containing residues Asp(463), Glu(534), and Glu(588), which are highly conserved among pUL89 homologs. Second, the model predicted a positively charged surface able to interact with the DNA duplex during the nicking event. Third, a hydrophobic patch on the top of the catalytic site suggested that this may constitute part of the pUL89 site recognized by pUL56 potentially involved in DNA binding.

PubMed: 20099308
DOI: 10.1002/prot.22669

実験手法

SOLUTION NMR