Abstract
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 A 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.
Publication types
-
Research Support, Non-U.S. Gov't
-
Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
-
Amino Acid Sequence
-
Animals
-
Base Sequence
-
Crystallography, X-Ray
-
DNA, Ribosomal / chemistry*
-
DNA, Ribosomal / metabolism
-
DNA-Binding Proteins / chemistry*
-
DNA-Binding Proteins / metabolism
-
Models, Molecular
-
Molecular Sequence Data
-
Nucleic Acid Conformation
-
Peptide Fragments / chemistry
-
Peptide Fragments / metabolism
-
Promoter Regions, Genetic
-
Protein Binding
-
Protein Conformation
-
RNA, Ribosomal, 5S*
-
Transcription Factor TFIIIA
-
Transcription Factors / chemistry*
-
Transcription Factors / metabolism
-
Xenopus laevis
-
Zinc Fingers*
Substances
-
DNA, Ribosomal
-
DNA-Binding Proteins
-
Peptide Fragments
-
RNA, Ribosomal, 5S
-
Transcription Factor TFIIIA
-
Transcription Factors