Prabu, J Rajan and Thamotharan, S and Khanduja, Jasbeer Singh and Alipio, Emily Zabala and Kim, Chang-Yub and Waldo, Geoffrey S and Terwilliger, Thomas C and Segelke, Brent and Lekin, Tim and Toppani, Dominique and Hung, Li-Wei and Yu, Minmin and Bursey, Evan Bursey and Muniyappa, K and Chandra, Nagasuma R and Vijayan, M (2006) Structure of Mycobacterium tuberculosis RuvA, a protein involved in recombination. In: Acta Crystallogr Sect F Struct Biol Cryst Commun, 62 (8). 731 -734.
sw5010.pdf - Published Version
Restricted to Registered users only
Download (264Kb) | Request a copy
The process of recombinational repair is crucial for maintaining genomic integrity and generating biological diversity. In association with RuvB and RuvC, RuvA plays a central role in processing and resolving Holliday junctions, which are a critical intermediate in homologous recombination. Here, the cloning, purification and structure determination of the RuvA protein from Mycobacterium tuberculosis (MtRuvA) are reported. Analysis of the structure and comparison with other known RuvA proteins reveal an octameric state with conserved subunit-subunit interaction surfaces, indicating the requirement of octamer formation for biological activity. A detailed analysis of plasticity in the RuvA molecules has led to insights into the invariant and variable regions, thus providing a framework for understanding regional flexibility in various aspects of RuvA function.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to National Center for Biotechnology Information.|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||24 Feb 2010 07:14|
|Last Modified:||19 Sep 2010 05:55|
Actions (login required)