TFIIIA FINGER 1-3 BOUND TO DNA, NMR, 22 STRUCTURESTFIIIA FINGER 1-3 BOUND TO DNA, NMR, 22 STRUCTURES

Structural highlights

1tf3 is a 3 chain structure with sequence from Xenopus laevis. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TF3A_XENLA Acts as both a positive transcription factor for 5S RNA genes and a specific RNA binding protein that complexes with 5S RNA in oocytes to form the 7S ribonucleoprotein storage particle. May play an essential role in the developmental change in 5S RNA gene expression. Interacts with the internal control region (ICR) of approximately 50 bases within the 5S RNA genes, is required for correct transcription of these genes by RNA polymerase III. Also binds the transcribed 5S RNA's.

Evolutionary Conservation

 

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The three N-terminal zinc fingers of transcription factor IIIA bind in the DNA major groove. Substantial packing interfaces are formed between adjacent fingers, the linkers lose their intrinsic flexibility upon DNA binding, and several lysine side chains implicated in DNA recognition are dynamically disordered.

Domain packing and dynamics in the DNA complex of the N-terminal zinc fingers of TFIIIA.,Foster MP, Wuttke DS, Radhakrishnan I, Case DA, Gottesfeld JM, Wright PE Nat Struct Biol. 1997 Aug;4(8):605-8. PMID:9253405[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Foster MP, Wuttke DS, Radhakrishnan I, Case DA, Gottesfeld JM, Wright PE. Domain packing and dynamics in the DNA complex of the N-terminal zinc fingers of TFIIIA. Nat Struct Biol. 1997 Aug;4(8):605-8. PMID:9253405
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