Unknown

Dataset Information

0

Structure of Mycobacterium tuberculosis RuvA, a protein involved in recombination.

ABSTRACT: 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.

SUBMITTER: Prabu JR 

PROVIDER: S-EPMC2242936 | biostudies-literature | 2006 Aug

REPOSITORIES: biostudies-literature

Json Xml
altmetric image

Publications

Structure of Mycobacterium tuberculosis RuvA, a protein involved in recombination.

Prabu J Rajan JR   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  

Acta crystallographica. Section F, Structural biology and crystallization communications 20060724 Pt 8

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 r  ...[more]

Similar Datasets

Unknown Evidence for recombination in Mycobacterium tuberculosis.
| S-EPMC1698211 | biostudies-literature
Unknown Ubiquitin-like protein involved in the proteasome pathway of Mycobacterium tuberculosis.
| S-EPMC2698935 | biostudies-literature
Unknown Structure of the MarR family protein Rv0880 from Mycobacterium tuberculosis.
| S-EPMC4461340 | biostudies-literature
Unknown Phylogeny of Mycobacterium tuberculosis Beijing strains constructed from polymorphisms in genes involved in DNA replication, recombination and repair.
| S-EPMC3024326 | biostudies-literature
Unknown Solution structure of the conserved hypothetical protein Rv2302 from Mycobacterium tuberculosis.
| S-EPMC1540057 | biostudies-literature
Unknown Crystal structure of Mycobacterium tuberculosis zinc-dependent metalloprotease-1 (Zmp1), a metalloprotease involved in pathogenicity.
| S-EPMC3173161 | biostudies-literature
Unknown Solution structure and refolding of the Mycobacterium tuberculosis pentapeptide repeat protein MfpA.
| S-EPMC2606005 | biostudies-literature
Unknown Crystal structure of Rv3899c(184-410), a hypothetical protein from Mycobacterium tuberculosis.
| S-EPMC4973306 | biostudies-literature
Unknown Structure and function of Rv0130, a conserved hypothetical protein from Mycobacterium tuberculosis.
| S-EPMC2242379 | biostudies-literature
Unknown Characterization of a novel heat shock protein (Hsp22.5) involved in the pathogenesis of Mycobacterium tuberculosis.
| S-EPMC3133320 | biostudies-literature