5KBJ

Structure of Rep-DNA complex

5KBJ の概要

• エントリーDOI: 10.2210/pdb5kbj/pdb
• 関連するPDBエントリー: 4PQK 4PQL 4PT7 4PTA
• 分子名称: Replication initiator A, N-terminal, DNA (32-MER) (3 entities in total)
• 機能のキーワード: replication initiation, rep protein, s. aureus, transcription-dna complex, transcription/dna
• 由来する生物種: Staphylococcus aureus; 詳細
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 147412.47

構造登録者

Schumacher, M. (登録日: 2016-06-03, 公開日: 2016-06-29, 最終更新日: 2023-09-27)

主引用文献

Schumacher, M.A.,Tonthat, N.K.,Kwong, S.M.,Chinnam, N.B.,Liu, M.A.,Skurray, R.A.,Firth, N.
Mechanism of staphylococcal multiresistance plasmid replication origin assembly by the RepA protein.
Proc. Natl. Acad. Sci. U.S.A., 111:9121-9126, 2014

PubMed Abstract: The staphylococcal multiresistance plasmids are key contributors to the alarming rise in bacterial multidrug resistance. A conserved replication initiator, RepA, encoded on these plasmids is essential for their propagation. RepA proteins consist of flexibly linked N-terminal (NTD) and C-terminal (CTD) domains. Despite their essential role in replication, the molecular basis for RepA function is unknown. Here we describe a complete structural and functional dissection of RepA proteins. Unexpectedly, both the RepA NTD and CTD show similarity to the corresponding domains of the bacterial primosome protein, DnaD. Although the RepA and DnaD NTD both contain winged helix-turn-helices, the DnaD NTD self-assembles into large scaffolds whereas the tetrameric RepA NTD binds DNA iterons using a newly described DNA binding mode. Strikingly, structural and atomic force microscopy data reveal that the NTD tetramer mediates DNA bridging, suggesting a molecular mechanism for origin handcuffing. Finally, data show that the RepA CTD interacts with the host DnaG primase, which binds the replicative helicase. Thus, these combined data reveal the molecular mechanism by which RepA mediates the specific replicon assembly of staphylococcal multiresistant plasmids.

PubMed: 24927575
DOI: 10.1073/pnas.1406065111

実験手法

X-RAY DIFFRACTION (3.09 Å)