Summary information and primary citation

PDB-id
8pop; SNAP-derived features in text and JSON formats; DNAproDB
Class
DNA binding protein
Method
cryo-EM (3.0 Å)
Summary
Hk97 small terminase in complex with DNA
Reference
Chechik M, Greive SJ, Antson AA, Jenkins HT (2023): "Structure of HK97 small terminase:DNA complex unveils a novel DNA binding mechanism by a circular protein." Biorxiv. doi: 10.1101/2023.07.17.549218.
Abstract
DNA recognition is critical for assembly of double-stranded DNA viruses, in particular for the initiation of packaging the viral genome into the capsid. DNA packaging has been extensively studied for three archetypal bacteriophage systems: cos , pac and phi29. We identified the minimal site within the cos region of bacteriophage HK97 specifically recognised by the small terminase and determined a cryoEM structure for the small terminase:DNA complex. This nonameric circular protein utilizes a previously unknown mechanism of DNA binding. While DNA threads through the central tunnel, unexpectedly, DNA-recognition is generated at its exit by a substructure formed by the N- and C-terminal segments of two adjacent protomers of the terminase which are unstructured in the absence of DNA. Such interaction ensures continuous engagement of the small terminase with DNA, allowing sliding along DNA while simultaneously checking the DNA sequence. This mechanism allows locating and instigating packaging initiation and termination precisely at the cos site.

Cartoon-block schematics in six views (download the tarball)

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