1G19

STRUCTURE OF RECA PROTEIN

1G19 の概要

• エントリーDOI: 10.2210/pdb1g19/pdb
• 分子名称: RECA PROTEIN, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: recombination, dna-repair, structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc, hydrolase
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37317.25

構造登録者

Datta, S.,Prabu, M.M.,Vaze, M.B.,Ganesh, N.,Chandra, N.R.,Muniyappa, K.,Vijayan, M.,TB Structural Genomics Consortium (TBSGC) (登録日: 2000-10-11, 公開日: 2000-12-11, 最終更新日: 2023-08-09)

主引用文献

Datta, S.,Prabu, M.M.,Vaze, M.B.,Ganesh, N.,Chandra, N.R.,Muniyappa, K.,Vijayan, M.
Crystal structures of Mycobacterium tuberculosis RecA and its complex with ADP-AlF(4): implications for decreased ATPase activity and molecular aggregation
Nucleic Acids Res., 28:4964-4973, 2000

PubMed Abstract: Sequencing of the complete genome of Mycobacterium tuberculosis, combined with the rapidly increasing need to improve tuberculosis management through better drugs and vaccines, has initiated extensive research on several key proteins from the pathogen. RecA, a ubiquitous multifunctional protein, is a key component of the processes of homologous genetic recombination and DNA repair. Structural knowledge of MtRecA is imperative for a full understanding of both these activities and any ensuing application. The crystal structure of MtRecA, presented here, has six molecules in the unit cell forming a 6(1) helical filament with a deep groove capable of binding DNA. The observed weakening in the higher order aggregation of filaments into bundles may have implications for recombination in mycobacteria. The structure of the complex reveals the atomic interactions of ADP-AlF(4), an ATP analogue, with the P-loop-containing binding pocket. The structures explain reduced levels of interactions of MtRecA with ATP, despite sharing the same fold, topology and high sequence similarity with EcRecA. The formation of a helical filament with a deep groove appears to be an inherent property of MtRecA. The histidine in loop L1 appears to be positioned appropriately for DNA interaction.

PubMed: 11121488
DOI: 10.1093/nar/28.24.4964

実験手法

X-RAY DIFFRACTION (3 Å)