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-Structure paper
タイトル | Structure of HK97 small terminase:DNA complex unveils a novel DNA binding mechanism by a circular protein. |
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ジャーナル・号・ページ | bioRxiv, Year 2023 |
掲載日 | 2023年7月20日 |
著者 | Maria Chechik / Sandra J Greive / Alfred A Antson / Huw T Jenkins / |
PubMed 要旨 | 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 ...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: , and phi29. We identified the minimal site within the 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 site. |
リンク | bioRxiv / PubMed:37503206 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.92 - 3.0 Å |
構造データ | EMDB-17794: HK97 small terminase in complex with DNA after focused classification EMDB-17818: Complex of HK97 small terminase with DNA |
由来 |
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キーワード | DNA BINDING PROTEIN (DNA結合タンパク質) / small terminase / HK97 / bacteriophage (ファージ) / complex with DNA |