Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.str.2013.11.007
Title: Architecture of a dsDNA viral capsid in complex with its maturation protease
Authors: Veesler, D.
Khayat, R.
Krishnamurthy, S.
Snijder, J.
Huang, R.K.
Heck, A.J.R.
Anand, G.S. 
Johnson, J.E.
Issue Date: 4-Feb-2014
Citation: Veesler, D., Khayat, R., Krishnamurthy, S., Snijder, J., Huang, R.K., Heck, A.J.R., Anand, G.S., Johnson, J.E. (2014-02-04). Architecture of a dsDNA viral capsid in complex with its maturation protease. Structure 22 (2) : 230-237. ScholarBank@NUS Repository. https://doi.org/10.1016/j.str.2013.11.007
Abstract: 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. © 2014 Elsevier Ltd.
Source Title: Structure
URI: http://scholarbank.nus.edu.sg/handle/10635/100116
ISSN: 09692126
DOI: 10.1016/j.str.2013.11.007
Appears in Collections:Staff Publications

Show full item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

18
checked on Nov 13, 2018

WEB OF SCIENCETM
Citations

17
checked on Nov 13, 2018

Page view(s)

41
checked on Oct 12, 2018

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.