Differing Roles for Zinc Fingers in DNA Recognition: Structure of a Six-Finger Transcription Factor IIIA Complex

The crystal structure of the six NH2-terminal zinc fingers of Xenopus laevis transcription factor IIIA (TFIIIA) bound with 31 bp of the 5S rRNA gene promoter has been determined at 3.1 angstrom resolution. Individual zinc fingers are positioned differently in the major groove and across the minor gr...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1998-03, Vol.95 (6), p.2938-2943
Main Authors: Nolte, Robert T., Conlin, Rachel M., Harrison, Stephen C., Brown, Raymond S.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino acids
Animals
Atoms
Base Sequence
Biological Sciences
Chemical bases
Crystal structure
Crystallography, X-Ray
Crystals
Datasets
Deoxyribonucleic acid
DNA
DNA, Ribosomal - chemistry
DNA, Ribosomal - metabolism
DNA-Binding Proteins - chemistry
DNA-Binding Proteins - metabolism
Genes
Models, Molecular
Molecular biology
Molecular Sequence Data
Nucleic Acid Conformation
Nucleic acids
Peptide Fragments - chemistry
Peptide Fragments - metabolism
Physics
Promoter Regions, Genetic
Protein Binding
Protein Conformation
RNA, Ribosomal, 5S
rRNA genes
Transcription Factor TFIIIA
Transcription factors
Transcription Factors - chemistry
Transcription Factors - metabolism
Xenopus laevis
Zinc
Zinc Fingers
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Summary:The crystal structure of the six NH2-terminal zinc fingers of Xenopus laevis transcription factor IIIA (TFIIIA) bound with 31 bp of the 5S rRNA gene promoter has been determined at 3.1 angstrom resolution. Individual zinc fingers are positioned differently in the major groove and across the minor groove of DNA to span the entire length of the duplex. These results show how TFIIIA can recognize several separated DNA sequences by using fewer fingers than necessary for continuous winding in the major groove.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.95.6.2938