2H5X

RuvA from Mycobacterium tuberculosis

Summary for 2H5X

• Entry DOI: 10.2210/pdb2h5x/pdb
• Descriptor: Holliday junction ATP-dependent DNA helicase ruvA, GLYCEROL (3 entities in total)
• Functional Keywords: recombination, ruva, holliday junction binding, dna binding protein
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 4
• Total formula weight: 81217.19

Authors

Prabu, J.R.,Thamotharan, S.,Khanduja, J.S.,Alipio, E.Z.,Kim, C.Y.,Waldo, G.S.,Terwilliger, T.C.,Segelke, B.,Lekin, T.,Toppani, D.,Hung, L.W.,Yu, M.,Bursey, E.,Muniyappa, K.,Chandra, N.R.,Vijayan, M. (deposition date: 2006-05-28, release date: 2006-08-15, Last modification date: 2023-08-30)

Primary citation

Prabu, J.R.,Thamotharan, S.,Khanduja, J.S.,Alipio, E.Z.,Kim, C.Y.,Waldo, G.S.,Terwilliger, T.C.,Segelke, B.,Lekin, T.,Toppani, D.,Hung, L.W.,Yu, M.,Bursey, E.,Muniyappa, K.,Chandra, N.R.,Vijayan, M.
Structure of Mycobacterium tuberculosis RuvA, a protein involved in recombination.
ACTA CRYSTALLOGR.,SECT.F, 62:731-734, 2006

PubMed 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.

PubMed: 16880543
DOI: 10.1107/S1744309106024791

Experimental method

X-RAY DIFFRACTION (2.7 Å)