1J9I

STRUCTURE OF THE DNA BINDING DOMAIN OF THE GPNU1 SUBUNIT OF LAMBDA TERMINASE

Summary for 1J9I

• Entry DOI: 10.2210/pdb1j9i/pdb
• NMR Information: BMRB: 4752
• Descriptor: TERMINASE SMALL SUBUNIT (1 entity in total)
• Functional Keywords: dna binding domain, homodimer, viral assembly, lambda, winged helix-turn-helix, terminase, viral protein
• Biological source: Enterobacteria phage lambda
• Total number of polymer chains: 2
• Total formula weight: 15637.54

Authors

De Beer, T.,Meyer, J.,Ortega, M.,Yang, Q.,Maes, L.,Duffy, C.,Berton, N.,Sippy, J.,Overduin, M.,Feiss, M.,Catalano, C. (deposition date: 2001-05-25, release date: 2002-08-14, Last modification date: 2024-05-22)

Primary citation

de Beer, T.,Fang, J.,Ortega, M.,Yang, Q.,Maes, L.,Duffy, C.,Berton, N.,Sippy, J.,Overduin, M.,Feiss, M.,Catalano, C.E.
Insights into specific DNA recognition during the assembly of a viral genome packaging machine.
Mol.Cell, 9:981-991, 2002

PubMed Abstract: Terminase enzymes mediate genome "packaging" during the reproduction of DNA viruses. In lambda, the gpNu1 subunit guides site-specific assembly of terminase onto DNA. The structure of the dimeric DNA binding domain of gpNu1 was solved using nuclear magnetic resonance spectroscopy. Its fold contains a unique winged helix-turn-helix (wHTH) motif within a novel scaffold. Surprisingly, a predicted P loop ATP binding motif is in fact the wing of the DNA binding motif. Structural and genetic analysis has identified determinants of DNA recognition specificity within the wHTH motif and the DNA recognition sequence. The structure reveals an unexpected DNA binding mode and provides a mechanistic basis for the concerted action of gpNu1 and Escherichia coli integration host factor during assembly of the packaging machinery.

PubMed: 12049735
DOI: 10.1016/S1097-2765(02)00537-3

Experimental method

SOLUTION NMR