3VEB

Crystal Structure of Matp-matS

3VEB の概要

• エントリーDOI: 10.2210/pdb3veb/pdb
• 関連するPDBエントリー: 3VEA 4D8J
• 分子名称: Macrodomain Ter protein, 5'-D(*TP*CP*GP*TP*GP*AP*CP*AP*TP*TP*GP*TP*CP*AP*CP*G)-3', 5'-D(*AP*CP*GP*TP*GP*AP*CP*AP*AP*TP*GP*TP*CP*AP*CP*G)-3', ... (5 entities in total)
• 機能のキーワード: macrodomains, chromosome, dna condensation, dna binding protein-dna complex, dna binding protein/dna
• 由来する生物種: Yersinia pestis
• 細胞内の位置: Cytoplasm (By similarity): Q8ZG78
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 45851.79

構造登録者

Schumacher, M.A. (登録日: 2012-01-07, 公開日: 2012-11-21, 最終更新日: 2024-02-28)

主引用文献

Dupaigne, P.,Tonthat, N.K.,Espeli, O.,Whitfill, T.,Boccard, F.,Schumacher, M.A.
Molecular basis for a protein-mediated DNA-bridging mechanism that functions in condensation of the E. coli chromosome.
Mol.Cell, 48:560-571, 2012

PubMed Abstract: The E. coli chromosome is condensed into insulated regions termed macrodomains (MDs), which are essential for genomic packaging. How chromosomal MDs are specifically organized and compacted is unknown. Here, we report studies revealing the molecular basis for Terminus-containing (Ter) chromosome condensation by the Ter-specific factor MatP. MatP contains a tripartite fold with a four-helix bundle DNA-binding motif, ribbon-helix-helix and C-terminal coiled-coil. Strikingly, MatP-matS structures show that the MatP coiled-coils form bridged tetramers that flexibly link distant matS sites. Atomic force microscopy and electron microscopy studies demonstrate that MatP alone loops DNA. Mutation of key coiled-coil residues destroys looping and causes a loss of Ter condensation in vivo. Thus, these data reveal the molecular basis for a protein-mediated DNA-bridging mechanism that mediates condensation of a large chromosomal domain in enterobacteria.

PubMed: 23084832
DOI: 10.1016/j.molcel.2012.09.009

実験手法

X-RAY DIFFRACTION (2.8 Å)