2007
DOI: 10.1016/j.jmb.2006.12.032
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Structure of the Escherichia coli Leucine-responsive Regulatory Protein Lrp Reveals a Novel Octameric Assembly

Abstract: The structure of Escherichia coli leucine-responsive regulatory protein (Lrp) cocrystallized with a short duplex oligodeoxynucleotide reveals a novel quaternary assembly in which the protein octamer forms an open, linear array of four dimers. In contrast, structures of the Lrp homologs LrpA, LrpC and AsnC crystallized in the absence of DNA show that these proteins instead form highly symmetrical octamers in which the four dimers form a closed ring. Although the DNA is disordered within the Lrp crystal, compara… Show more

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Cited by 90 publications
(131 citation statements)
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“…High affinity Ptr2 binding to this UAS stems, at least in part, from its compliance with tight DNA wrapping around the Ptr2 tetramer/octamer, with concomitant bending and narrowing of the minor groove at the dyad centers of the binding sites (Fig. 5C, Vertical Arrows); these are known features of the binding sites of both the bacterial and archaeal Lrp/AsnC family proteins (25)(26)(27)(28)(29)(30). It is therefore likely that these same sequence features also accommodate efficient positioning of histones within the synthetically optimized UAS.…”
Section: Resultsmentioning
confidence: 99%
“…High affinity Ptr2 binding to this UAS stems, at least in part, from its compliance with tight DNA wrapping around the Ptr2 tetramer/octamer, with concomitant bending and narrowing of the minor groove at the dyad centers of the binding sites (Fig. 5C, Vertical Arrows); these are known features of the binding sites of both the bacterial and archaeal Lrp/AsnC family proteins (25)(26)(27)(28)(29)(30). It is therefore likely that these same sequence features also accommodate efficient positioning of histones within the synthetically optimized UAS.…”
Section: Resultsmentioning
confidence: 99%
“…Lrp is the closest analog to a eukaryotic histone. Lrp forms octomeric structures around which DNA winds, similarly to DNA wrapping around histones (de los Rios and Perona 2007). HU, IHF, Lrp, DnaA, and IciA are also global transcription regulators (Bouvier et al 1998;Oberto et al 2009;Prieto et al 2012).…”
mentioning
confidence: 99%
“…UPEC Lrp binds to three of the six Lrp binding sites in the pap promoter; binding of proximal sites leads to the pap off state, while binding of distal sites results in the on state (73). Cocrystal structures of Lrp with pap promoter DNA reveal that DNA wraps around and binds to an octameric Lrp complex, reminiscent of the eukaryotic nucleosome-like complex (74)(75)(76). Therefore, Lrp multimerization and DNA topology are crucial for transcriptional regulation, providing a mechanistic rationale for how changes in Lrp concentrations could influence phenotypic variation of symbiotic phenotypes in X. nematophila.…”
Section: Phenotypic Variation In X Nematophilamentioning
confidence: 99%