Snapshots of a molecular swivel in action

Trejo, C. S., Rock, R. S., Stark, W. M. , Boocock, M. R. and Rice, P. A. (2018) Snapshots of a molecular swivel in action. Nucleic Acids Research, 46(10), pp. 5286-5296. (doi: 10.1093/nar/gkx1309) (PMID:29315406) (PMCID:PMC6007550)

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Members of the serine family of site-specific recombinases exchange DNA strands via 180° rotation about a central protein-protein interface. Modeling of this process has been hampered by the lack of structures in more than one rotational state for any individual serine recombinase. Here we report crystal structures of the catalytic domains of four constitutively active mutants of the serine recombinase Sin, providing snapshots of rotational states not previously visualized for Sin, including two seen in the same crystal. Normal mode analysis predicted that each tetramer's lowest frequency mode (i.e. most accessible large-scale motion) mimics rotation: two protomers rotate as a pair with respect to the other two. Our analyses also suggest that rotation is not a rigid body movement around a single symmetry axis but instead uses multiple pivot points and entails internal motions within each subunit.

Item Type:Articles
Glasgow Author(s) Enlighten ID:Stark, Professor Marshall and Boocock, Dr Martin
Authors: Trejo, C. S., Rock, R. S., Stark, W. M., Boocock, M. R., and Rice, P. A.
College/School:College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
Journal Name:Nucleic Acids Research
Publisher:Oxford University Press
ISSN (Online):1362-4962
Published Online:05 January 2018
Copyright Holders:Copyright © 2018 The Authors
First Published:First published in Nucleic Acids Research 46(10): 5286-5296
Publisher Policy:Reproduced under a Creative Commons License

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