1exe

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1exe.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1exe.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{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==
+
<!--
-
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.
 +
-->
 +
{{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==
Line 29: Line 33:
[[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

Image: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

Page seeded by OCA on Tue Jul 1 02:10:00 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1exe"
Personal tools