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Plasmid replication initiator RepB forms a hexamer reminiscent of ring helicases and has mobile nuclease domains

AuthorsBoer, Roeland ; Ruiz-Masó, José A. ; López-Blanco, José R.; Chacón, Pablo ; Usón, Isabel ; Espinosa, Manuel ; Llorca, Óscar ; Solar, Gloria del
KeywordsDNA-binding protein
Plasmid replication
Replication initiator
X-ray crystal structure
Issue Date3-Jun-2009
CitationEMBO Journal, 28: 1666-1678 (2009)
AbstractRepB initiates plasmid rolling-circle replication by binding to a triple 11-bp direct repeat (bind locus) and cleaving the DNA at a specific distant site located in a hairpin loop within the nic locus of the origin. The structure of native full-length RepB reveals a hexameric ring molecule, where each protomer has two domains. The origin-binding and catalytic domains show a three-layer α–β–α sandwich fold. The active site is positioned at one of the faces of the β-sheet and coordinates a Mn2+ ion at short distance from the essential nucleophilic Y99. The oligomerization domains (ODs), each consisting of four α-helices, together define a compact ring with a central channel, a feature found in ring helicases. The toroidal arrangement of RepB suggests that, similar to ring helicases, it encircles one of the DNA strands during replication to confer processivity to the replisome complex. The catalytic domains appear to be highly mobile with respect to ODs. This mobility may account for the adaptation of the protein to two distinct DNA recognition sites
Description47 p.-7 fig. Boer, Roeland et alt.
Publisher version (URL)http://dx.doi.org/10.1038/emboj.2009.125
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