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-Structure paper
タイトル | Architecture of a dsDNA viral capsid in complex with its maturation protease. |
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ジャーナル・号・ページ | Structure, Vol. 22, Issue 2, Page 230-237, Year 2014 |
掲載日 | 2014年2月4日 |
著者 | David Veesler / Reza Khayat / Srinath Krishnamurthy / Joost Snijder / Rick K Huang / Albert J R Heck / Ganesh S Anand / John E Johnson / |
PubMed 要旨 | Most double-stranded DNA (dsDNA) viruses, including bacteriophages and herpesviruses, rely on a staged assembly process of capsid formation. A viral protease is required for many of them to ...Most double-stranded DNA (dsDNA) viruses, including bacteriophages and herpesviruses, rely on a staged assembly process of capsid formation. A viral protease is required for many of them to disconnect scaffolding domains/proteins from the capsid shell, therefore priming the maturation process. We used the bacteriophage HK97 as a model system to decipher the molecular mechanisms underlying the recruitment of the maturation protease by the assembling procapsid and the influence exerted onto the latter. Comparisons of the procapsid with and without protease using single-particle cryoelectron microscopy reconstructions, hydrogen/deuterium exchange coupled to mass spectrometry, and native mass spectrometry demonstrated that the protease interacts with the scaffolding domains within the procapsid interior and stabilizes them as well as the whole particle. The results suggest that the thermodynamic consequences of protease packaging are to shift the equilibrium between isolated coat subunit capsomers and procapsid in favor of the latter by stabilizing the assembled particle before making the process irreversible through proteolysis of the scaffolding domains. |
リンク | Structure / PubMed:24361271 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 7.8 - 8.3 Å |
構造データ | EMDB-5828: EMDB-5829: |