1dvo
THE X-RAY CRYSTAL STRUCTURE OF FINO, A REPRESSOR OF BACTERIAL CONJUGATION
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OverviewOverview
The conjugative transfer of F-like plasmids is repressed by FinO, an RNA, binding protein. FinO interacts with the F-plasmid encoded traJ mRNA and, its antisense RNA, FinP, stabilizing FinP against endonucleolytic, degradation and facilitating sense-antisense RNA recognition. Here we, present the 2.0 A resolution X-ray crystal structure of FinO, lacking its, flexible N-terminal extension. FinO adopts a novel, elongated, largely, helical conformation. An N-terminal region, previously shown to contact, RNA, forms a positively charged alpha-helix (helix 1) that protrudes 45 A, from the central core of FinO. A C-terminal region of FinO that is, implicated in RNA interactions also extends out from the central body of, the protein, adopting a helical conformation and packing against the base, of the N-terminal helix. A highly positively charged patch on the surface, of the FinO core may present another RNA binding surface. The results of, an in vitro RNA duplexing assay demonstrate that the flexible N-terminal, region of FinO plays a key role in FinP-traJ RNA recognition, and supports, our proposal that this region and the N-terminus of helix 1 interact with, and stabilize paired, complementary RNA loops in a kissing complex.
About this StructureAbout this Structure
1DVO is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the bacterial conjugation repressor finO., Ghetu AF, Gubbins MJ, Frost LS, Glover JN, Nat Struct Biol. 2000 Jul;7(7):565-9. PMID:10876242
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