1exe
From Proteopedia
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'''SOLUTION STRUCTURE OF A MUTANT OF TRANSCRIPTION FACTOR 1.''' | '''SOLUTION STRUCTURE OF A MUTANT OF TRANSCRIPTION FACTOR 1.''' | ||
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[[Category: Liu, W.]] | [[Category: Liu, W.]] | ||
[[Category: Vu, H M.]] | [[Category: Vu, H M.]] | ||
| - | [[Category: | + | [[Category: Beta ribbon arm]] |
| - | [[Category: | + | [[Category: Dna-bending protein]] |
| - | [[Category: | + | [[Category: Dna-binding]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:38:03 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 12:38, 2 May 2008
SOLUTION STRUCTURE OF A MUTANT OF TRANSCRIPTION FACTOR 1.
Overview
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.
About this Structure
1EXE is a Single protein structure of sequence from Spiroplasma phage 4. Full crystallographic information is available from OCA.
Reference
Solution structure of a mutant of transcription factor 1: implications for enhanced DNA binding., Liu W, Vu HM, Geiduschek EP, Kearns DR, J Mol Biol. 2000 Sep 29;302(4):821-30. PMID:10993726 Page seeded by OCA on Fri May 2 15:38:03 2008
