Structural basis for DNA recognition and loading into a viral packaging motor.

Journal article

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 assem...

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Authors: Büttner, C; Chechik, M; Ortiz-Lombardía, M; Smits, C; Ebong, I

• Publication status: Published
• Journal: Proceedings of the National Academy of Sciences of the United States of America
• Volume: 109
• Issue: 3
• Pages: 811-816
• Publication date: 2012-01-01
• DOI: 10.1073/pnas.1110270109
• EISSN: 1091-6490
• ISSN: 0027-8424
• Language: English
• Keywords: Sequence Deletion; Models, Molecular; Virus Assembly; Protein Subunits; Protein Multimerization; Siphoviridae; Protein Binding; Endodeoxyribonucleases; DNA; Protein Structure, Tertiary; Molecular Motor Proteins; Protein Structure, Secondary; Mass Spectrometry