3VEB

Crystal Structure of Matp-matS

Summary for 3VEB

• Entry DOI: 10.2210/pdb3veb/pdb
• Related: 3VEA 4D8J
• Descriptor: 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)
• Functional Keywords: macrodomains, chromosome, dna condensation, dna binding protein-dna complex, dna binding protein/dna
• Biological source: Yersinia pestis
• Cellular location: Cytoplasm (By similarity): Q8ZG78
• Total number of polymer chains: 4
• Total formula weight: 45851.79

Authors

Schumacher, M.A. (deposition date: 2012-01-07, release date: 2012-11-21, Last modification date: 2024-02-28)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.8 Å)