3vea | pdb_00003vea

Crystal Structure of matP-matS23mer

spinqualitylabelsall models 3vea, resolution 2.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3vea is a 4 chain structure with sequence from Yersinia pestis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 3veb, 4d8j Gene: matP, y2737, YPO1433, YP_0877 (Yersinia pestis) Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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. Molecular Basis for a Protein-Mediated DNA-Bridging Mechanism that Functions in Condensation of the E. coli Chromosome.,Dupaigne P, Tonthat NK, Espeli O, Whitfill T, Boccard F, Schumacher MA Mol Cell. 2012 Oct 16. pii: S1097-2765(12)00785-X. doi:, 10.1016/j.molcel.2012.09.009. PMID:23084832 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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