1EXE

SOLUTION STRUCTURE OF A MUTANT OF TRANSCRIPTION FACTOR 1.

Summary for 1EXE

• Entry DOI: 10.2210/pdb1exe/pdb
• Related: 1WTU
• Descriptor: TRANSCRIPTION FACTOR 1 (1 entity in total)
• Functional Keywords: beta ribbon arms, dna-binding, dna-bending protein, transcription
• Biological source: Bacillus phage SPO1
• Total number of polymer chains: 2
• Total formula weight: 21384.76

Authors

Liu, W.,Vu, H.M.,Geiduschek, E.P.,Kearns, D.R. (deposition date: 2000-05-02, release date: 2000-10-18, Last modification date: 2024-05-22)

Primary citation

Liu, W.,Vu, H.M.,Geiduschek, E.P.,Kearns, D.R.
Solution structure of a mutant of transcription factor 1: implications for enhanced DNA binding.
J.Mol.Biol., 302:821-830, 2000

PubMed Abstract: An NMR solution structure of a mutant of the homodimer protein transcription factor 1, TF1-G15/I32 (22 kDa), has been solved to atomic resolution, with 23 final structures that converge to an r.m. s.d. of 0.78 A. The overall shape of TF1-G15/I32 remains similar to that of the wild-type protein and other type II DNA-binding proteins. Each monomer has two N-terminal alpha-helices separated by a short loop, followed by a three-stranded beta-sheet, whose extension between the second and third beta-strands forms an antiparallel beta-ribbon arm, leading to a C-terminal third alpha-helix that is severely kinked in the middle. Close examination of the structure of TF1-G15/I32 reveals why it is more stable and binds DNA more tightly than does its wild-type counterpart. The dimeric core, consisting of the N-terminal helices and the beta-sheets, is more tightly packed, and this might be responsible for its increased thermal stability. The DNA-binding domain, composed of the top face of the beta-sheet, the beta-ribbon arms and the C-terminal helices, is little changed from wild-type TF1. Rather, the enhancement in DNA affinity must be due almost exclusively to the creation of an additional DNA-binding site at the side of the dimer by changes affecting helices 1 and 2: helix 2 of TF1-G15/I32 is one residue longer than helix 2 of the wild-type protein, bends inward, and is both translationally and rotationally displaced relative to helix 1. This rearrangement creates a longer, narrower fissure between the V-shaped N-terminal helices and exposes additional positively charged surface at each side of the dimer.

PubMed: 10993726
DOI: 10.1006/jmbi.2000.4084

Experimental method

SOLUTION NMR