| Literature DB >> 18621389 |
Sebyung Kang1, Anton Poliakov, Jennifer Sexton, Matthew B Renfrow, Peter E Prevelige.
Abstract
The Double-stranded DNA bacteriophage P22 has a ring-shaped dodecameric complex composed of the 84 kDa portal protein subunit that forms the central channel of the phage DNA packaging motor. The overall morphology of the P22 portal complex is similar to that of the portal complexes of Phi29, SPP1, T3, T7 phages and herpes simplex virus. Secondary structure prediction of P22 portal protein and its threading onto the crystal structure of the Phi29 portal complexes suggested that the P22 portal protein complex shares conserved helical modules that were found in the dodecameric interfaces of the Phi29 portal complex. To identify the amino acids involved in intersubunit contacts in the P22 portal ring complexes and validate the threading model, we performed comparative hydrogen/deuterium exchange analysis of monomeric and in vitro assembled portal proteins of P22 and the dodecameric Phi29 portal. Hydrogen/deuterium exchange experiments provided evidence of intersubunit interactions in the P22 portal complex similar to those in the Phi29 portal that map to the regions predicted to be conserved helical modules.Entities:
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Year: 2008 PMID： 18621389 PMCID： PMC2593103 DOI： 10.1016/j.jmb.2008.03.004
Source DB: PubMed Journal: J Mol Biol ISSN： 0022-2836 Impact factor: 5.469