2BKE

Conformational Flexibility Revealed by the Crystal Structure of a Crenarchaeal RadA

2BKE の概要

• エントリーDOI: 10.2210/pdb2bke/pdb
• 分子名称: DNA REPAIR AND RECOMBINATION PROTEIN RADA, CHLORIDE ION (3 entities in total)
• 機能のキーワード: dna-binding protein, homologous recombination, dna repair, filament, rada, rad51, reca, sulfolobus solfataricus, archaea, dna-binding protei, dna binding protein
• 由来する生物種: SULFOLOBUS SOLFATARICUS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36277.75

構造登録者

Ariza, A.,Richard, D.L.,White, M.F.,Bond, C.S. (登録日: 2005-02-15, 公開日: 2005-03-16, 最終更新日: 2024-10-09)

主引用文献

Ariza, A.,Richard, D.L.,White, M.F.,Bond, C.S.
Conformational Flexibility Revealed by the Crystal Structure of a Crenarchaeal Rada
Nucleic Acids Res., 33:1465-, 2005

PubMed Abstract: Homologous recombinational repair is an essential mechanism for repair of double-strand breaks in DNA. Recombinases of the RecA-fold family play a crucial role in this process, forming filaments that utilize ATP to mediate their interactions with single- and double-stranded DNA. The recombinase molecules present in the archaea (RadA) and eukaryota (Rad51) are more closely related to each other than to their bacterial counterpart (RecA) and, as a result, RadA makes a suitable model for the eukaryotic system. The crystal structure of Sulfolobus solfataricus RadA has been solved to a resolution of 3.2 A in the absence of nucleotide analogues or DNA, revealing a narrow filamentous assembly with three molecules per helical turn. As observed in other RecA-family recombinases, each RadA molecule in the filament is linked to its neighbour via interactions of a short beta-strand with the neighbouring ATPase domain. However, despite apparent flexibility between domains, comparison with other structures indicates conservation of a number of key interactions that introduce rigidity to the system, allowing allosteric control of the filament by interaction with ATP. Additional analysis reveals that the interaction specificity of the five human Rad51 paralogues can be predicted using a simple model based on the RadA structure.

PubMed: 15755748
DOI: 10.1093/NAR/GKI288

実験手法

X-RAY DIFFRACTION (3.2 Å)