Structure of Mycobacterium tuberculosis RuvA, a protein involved in recombination

Journal Article · Tue Aug 01 00:00:00 EDT 2006 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S1744309106024791· OSTI ID:22360190

Prabu, J. Rajan; Thamotharan, S. ^[1]; Khanduja, Jasbeer Singh ^[2]; Alipio, Emily Zabala; Kim, Chang-Yub; Waldo, Geoffrey S.; Terwilliger, Thomas C. ^[3]; Segelke, Brent; Lekin, Tim; Toppani, Dominique ^[4]; Hung, Li-Wei ^[5]; Yu, Minmin; Bursey, Evan ^[6]; Muniyappa, K. ^[2]

---

1. Molecular Biophysics Unit, Indian Institute of Science, Bangalore (India)
2. Department of Biochemistry, Indian Institute of Science, Bangalore (India)
3. Bioscience Division, Los Alamos National Laboratory, Los Alamos (United States)
4. Biology and Biotechnology Program, Lawrence Livermore National Laboratory, Livermore (United States)
5. Physics Division, Los Alamos National Laboratory, Los Alamos (United States)
6. Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley (United States)

RuvA, a protein from M. tuberculosis H37Rv involved in recombination, has been cloned, expressed, purified and analysed by X-ray crystallography. 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.

• OSTI ID: 22360190
• Journal Information: Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 8 Vol. 62; ISSN ACSFCL; ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
CRYSTALLOGRAPHY
FLEXIBILITY
INTERACTIONS
MOLECULES
PLASTICITY
PROCESSING
PROTEINS
RECOMBINATION
SURFACES