A docking model based on mass spectrometric and biochemical data describes phage packaging motor incorporation.

ABSTRACT: The molecular mechanism of scaffolding protein-mediated incorporation of one and only one DNA packaging motor/connector dodecamer at a unique vertex during lambdoid phage assembly has remained elusive because of the lack of structural information on how the connector and scaffolding proteins interact. We assembled and characterized a phi29 connector-scaffolding complex, which can be incorporated into procapsids during in vitro assembly. Native mass spectrometry revealed that the connector binds at most 12 scaffolding molecules, likely organized as six dimers. A data-driven docking model, using input from chemical cross-linking and mutagenesis data, suggested an interaction between the scaffolding protein and the exterior of the wide domain of the connector dodecamer. The connector binding

SUBMITTER: Fu CY 

PROVIDER: S-EPMC2938058 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature