Title

Authors

Affiliation

¹School of Biotechnology, Lovely Professional University, Phagwara, Punjab-144402, India; ²Biosciences group, Birla Institute of Technology and Science-Pilani, Hyderabad Campus, Shamirpet, Andhra Pradesh-500078, India; ³Center for Computational Natural Sciences and Bioinformatics, International Institute of Information Technology, Hyderabad-500032, India

Email

nishtha.13391@lpu.co.in; *Corresponding author

Article Type

Hypothesis

Date

Received November 29, 2011; Accepted December 5, 2011; Published December 21, 2011

RecQ helicases feature multiple domains in their structure, of which the helicase domain, the RecQ-Ct domain and the HRDC domains are well conserved among the SF2 helicases. The helicase domain and the RecQ-Ct domain constitute the catalytic core of the enzyme. The domain interfaces are the DNA binding sites which display significant conformational changes in our molecular dynamics simulation studies. The preferred conformational states of the DNA bound and unbound forms of RecQ appear to be quite different from each other. DNA binding induces inter-domain flexibility leading to hinge mobility between the domains. The divergence in the dynamics of the two structures is caused by changes in the interactions at the domain interface, which seems to propagate along the whole protein structure. This could be essential in ssDNA binding after strand separation, as well as aiding translocation of the RecQ protein like an inch-worm.

Keywords

Helicase mechanism, Homology modeling, Molecular Dynamics simulations, Unwinding, Translocation.

Citation

Pandey et al. Bioinformation 7(8): 371-374 (2011)
 

Edited by

P Kangueane

ISSN

0973-2063

Publisher

Biomedical Informatics

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.