1DVO

THE X-RAY CRYSTAL STRUCTURE OF FINO, A REPRESSOR OF BACTERIAL CONJUGATION

Summary for 1DVO

• Entry DOI: 10.2210/pdb1dvo/pdb
• Descriptor: FERTILITY INHIBITION PROTEIN O (2 entities in total)
• Functional Keywords: repressor, bacterial conjugation, transcription
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 17374.12

Authors

Ghetu, A.F.,Gubbins, M.J.,Frost, L.S.,Glover, J.N.M. (deposition date: 2000-01-21, release date: 2000-07-19, Last modification date: 2024-02-07)

Primary citation

Ghetu, A.F.,Gubbins, M.J.,Frost, L.S.,Glover, J.N.
Crystal structure of the bacterial conjugation repressor finO.
Nat.Struct.Biol., 7:565-569, 2000

PubMed Abstract: 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.

PubMed: 10876242
DOI: 10.1038/76790

Experimental method

X-RAY DIFFRACTION (2 Å)