Structure of Mycobacterium tuberculosis RuvA, a protein involved in recombination.
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.
Prabu
J Rajan
JR
Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India.
Thamotharan
S
S
Khanduja
Jasbeer Singh
JS
Alipio
Emily Zabala
EZ
Kim
Chang Yub
CY
Waldo
Geoffrey S
GS
Terwilliger
Thomas C
TC
Segelke
Brent
B
Lekin
Tim
T
Toppani
Dominique
D
Hung
Li Wei
LW
Yu
Minmin
M
Bursey
Evan
E
Muniyappa
K
K
Chandra
Nagasuma R
NR
Vijayan
M
M
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics*; D001665:Binding Sites; D018360:Crystallography, X-Ray; D004265:DNA Helicases / Q000737:chemistry* / Q000235:genetics*; D008958:Models, Molecular; D009169:Mycobacterium tuberculosis / Q000235:genetics*; D011487:Protein Conformation; D011995:Recombination, Genetic
D001426:Bacterial Proteins; D004265:DNA Helicases