2KN8

NMR structure of the C-terminal domain of pUL89

Summary for 2KN8

• Entry DOI: 10.2210/pdb2kn8/pdb
• NMR Information: BMRB: 16452
• Descriptor: DNA cleavage and packaging protein large subunit, UL89 (1 entity in total)
• Functional Keywords: nhcmv, pul89, terminase, protein binding, dna binding protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 7916.91

Authors

Couvreux, A.,Hantz, S.,Marquant, R.,Champier, G.,Alain, S.,Morellet, N.,Bouaziz, S. (deposition date: 2009-08-18, release date: 2010-06-09, Last modification date: 2024-05-01)

Primary citation

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

Experimental method

SOLUTION NMR