1exe: Difference between revisions

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[[Image:1exe.gif|left|200px]]
{{Seed}}
[[Image:1exe.png|left|200px]]


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{{STRUCTURE_1exe|  PDB=1exe  |  SCENE=  }}  
{{STRUCTURE_1exe|  PDB=1exe  |  SCENE=  }}  


'''SOLUTION STRUCTURE OF A MUTANT OF TRANSCRIPTION FACTOR 1.'''
===SOLUTION STRUCTURE OF A MUTANT OF TRANSCRIPTION FACTOR 1.===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_10993726}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 10993726 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10993726}}


==About this Structure==
==About this Structure==
1EXE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Spiroplasma_phage_4 Spiroplasma phage 4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EXE OCA].  
1EXE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Spiroplasma_phage_4 Spiroplasma phage 4]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EXE OCA].  


==Reference==
==Reference==
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[[Category: Dna-bending protein]]
[[Category: Dna-bending protein]]
[[Category: Dna-binding]]
[[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 Tue Jul 1 02:10:00 2008''

Revision as of 23:10, 30 June 2008

File:1exe.png

Template:STRUCTURE 1exe

SOLUTION STRUCTURE OF A MUTANT OF TRANSCRIPTION FACTOR 1.

Template:ABSTRACT PUBMED 10993726

About this Structure

1EXE is a Single protein structure of sequence from Spiroplasma phage 4. Full experimental 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

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