1hkq
From Proteopedia
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PPS10 PLASMID DNA REPLICATION INITIATOR PROTEIN REPA. REPLICATION INACTIVE, DIMERIC N-TERMINAL DOMAIN.
Overview
Plasmids are natural vectors for gene transfer. In Gram-negative bacteria, plasmid DNA replication is triggered when monomers of an initiator protein, (Rep) bind to direct repeats at the origin sequence. Rep dimers, which are, inactive as initiators, bind to an inverse repeat operator, repressing, transcription of the rep gene. Rep proteins are composed of N-terminal, dimerization and C-terminal DNA-binding domains. Activation of Rep is, coupled to dimer dissociation, converting the dimerization domain into a, second origin-binding module. Although the structure of the monomeric F, plasmid initiator (mRepE) has been determined, the molecular nature of Rep, activation remains unknown. Here we report the crystal structure of the, dimeric N-terminal domain of the pPS10 plasmid initiator (dRepA). dRepA, has a winged-helix fold, as does its homologous domain in mRepE. However, dimerization transforms an interdomain loop and beta-strand (monomeric, RepE) into an alpha-helix (dimeric RepA). dRepA resemble the C terminus of, eukaryotic and archaeal Cdc6, giving clues to the phylogeny of DNA, replication initiators.
About this Structure
1HKQ is a Single protein structure of sequence from Pseudomonas savastanoi with , and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
A conformational switch between transcriptional repression and replication initiation in the RepA dimerization domain., Giraldo R, Fernandez-Tornero C, Evans PR, Diaz-Orejas R, Romero A, Nat Struct Biol. 2003 Jul;10(7):565-71. PMID:12766757
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