Probing conserved helical modules of portal complexes by mass spectrometry-based hydrogen/deuterium exchange
Cited 9 times inCited 8 times in
- Probing conserved helical modules of portal complexes by mass spectrometry-based hydrogen/deuterium exchange
- Kang, Sebyung; Poliakov, Anton; Sexton, Jennifer; Renfrow, Matthew B.; Prevelige, Peter E., Jr.
- bacteriophage P22; hydrogen exchange; mass spectrometry; portal protein; virus
- Issue Date
- ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
- JOURNAL OF MOLECULAR BIOLOGY, v.381, no.3, pp.772 - 784
- The Double-stranded DNA bacteriophage P22 has a ring-shaped dodecameric complex composed of the 84 kDa porta I 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.
- ; Go to Link
Appears in Collections:
- SLS_Journal Papers
can give you direct access to the published full text of this article. (UNISTARs only)
Show full item record
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.