3vea
From Proteopedia
Crystal Structure of matP-matS23mer
Structural highlights
Function[MATP_YERPE] Required for spatial organization of the terminus region of the chromosome (Ter macrodomain) during the cell cycle. Prevents early segregation of duplicated Ter macrodomains during cell division. Binds specifically to matS, which is a 13 bp signature motif repeated within the Ter macrodomain.[HAMAP-Rule:MF_01073] Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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