4GCL

structure of no-dna factor

4GCL の概要

• エントリーDOI: 10.2210/pdb4gcl/pdb
• 関連するPDBエントリー: 4GCK 4GCT 4GCU 4GFK 4GFL
• 分子名称: Nucleoid occlusion factor SlmA, DNA (5'-D(*AP*GP*TP*GP*AP*GP*TP*AP*CP*TP*CP*AP*CP*T)-3'), 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (4 entities in total)
• 機能のキーワード: dna binding protein, dna binding protein-dna complex, dna binding protein/dna
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm, nucleoid (By similarity): Q1R4V1
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 212469.34

構造登録者

Schumacher, M.A. (登録日: 2012-07-30, 公開日: 2013-06-19, 最終更新日: 2024-02-28)

主引用文献

Tonthat, N.K.,Milam, S.L.,Chinnam, N.,Whitfill, T.,Margolin, W.,Schumacher, M.A.
SlmA forms a higher-order structure on DNA that inhibits cytokinetic Z-ring formation over the nucleoid.
Proc.Natl.Acad.Sci.USA, 110:10586-10591, 2013

PubMed Abstract: The spatial and temporal control of Filamenting temperature sensitive mutant Z (FtsZ) Z-ring formation is crucial for proper cell division in bacteria. In Escherichia coli, the synthetic lethal with a defective Min system (SlmA) protein helps mediate nucleoid occlusion, which prevents chromosome fragmentation by binding FtsZ and inhibiting Z-ring formation over the nucleoid. However, to perform its function, SlmA must be bound to the nucleoid. To deduce the basis for this chromosomal requirement, we performed biochemical, cellular, and structural studies. Strikingly, structures show that SlmA dramatically distorts DNA, allowing it to bind as an orientated dimer-of-dimers. Biochemical data indicate that SlmA dimer-of-dimers can spread along the DNA. Combined structural and biochemical data suggest that this DNA-activated SlmA oligomerization would prevent FtsZ protofilament propagation and bundling. Bioinformatic analyses localize SlmA DNA sites near membrane-tethered chromosomal regions, and cellular studies show that SlmA inhibits FtsZ reservoirs from forming membrane-tethered Z rings. Thus, our combined data indicate that SlmA DNA helps block Z-ring formation over chromosomal DNA by forming higher-order protein-nucleic acid complexes that disable FtsZ filaments from coalescing into proper structures needed for Z-ring creation.

PubMed: 23754405
DOI: 10.1073/pnas.1221036110

実験手法

X-RAY DIFFRACTION (2.65 Å)