1trr
From Proteopedia
(New page: 200px<br /><applet load="1trr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1trr, resolution 2.400Å" /> '''TANDEM BINDING IN C...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1trr.gif|left|200px]]<br /><applet load="1trr" size=" | + | [[Image:1trr.gif|left|200px]]<br /><applet load="1trr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1trr, resolution 2.400Å" /> | caption="1trr, resolution 2.400Å" /> | ||
'''TANDEM BINDING IN CRYSTALS OF A TRP REPRESSOR/OPERATOR HALF-SITE COMPLEX'''<br /> | '''TANDEM BINDING IN CRYSTALS OF A TRP REPRESSOR/OPERATOR HALF-SITE COMPLEX'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of trp repressor tandemly bound in a 2:1 complex to | + | The crystal structure of trp repressor tandemly bound in a 2:1 complex to a 16-base-pair palindromic DNA containing a central trp operator half-site has been determined and refined to 2.4 A resolution. Despite dramatically different DNA sequence contexts and crystallization conditions, the protein/DNA interface is essentially identical to that seen in the original trp repressor/operator complex structure. Water-mediated sequence recognition by trp repressor is likely to be related to the unusual end-on approach of the recognition helix (E), which allows sharing of the major groove by tandem dimers. The tandem complex model accounts for the mutational sensitivity of all trp operator base pairs. The structure also provides the first detailed view of the tandem interaction, revealing a key role for the amino-terminal arms. |
==About this Structure== | ==About this Structure== | ||
| - | 1TRR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with TRP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1TRR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=TRP:'>TRP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TRR OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Carey, J.]] | [[Category: Carey, J.]] | ||
| - | [[Category: Lawson, C | + | [[Category: Lawson, C L.]] |
[[Category: TRP]] | [[Category: TRP]] | ||
[[Category: protein-dna complex]] | [[Category: protein-dna complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:16:40 2008'' |
Revision as of 13:16, 21 February 2008
|
TANDEM BINDING IN CRYSTALS OF A TRP REPRESSOR/OPERATOR HALF-SITE COMPLEX
Overview
The crystal structure of trp repressor tandemly bound in a 2:1 complex to a 16-base-pair palindromic DNA containing a central trp operator half-site has been determined and refined to 2.4 A resolution. Despite dramatically different DNA sequence contexts and crystallization conditions, the protein/DNA interface is essentially identical to that seen in the original trp repressor/operator complex structure. Water-mediated sequence recognition by trp repressor is likely to be related to the unusual end-on approach of the recognition helix (E), which allows sharing of the major groove by tandem dimers. The tandem complex model accounts for the mutational sensitivity of all trp operator base pairs. The structure also provides the first detailed view of the tandem interaction, revealing a key role for the amino-terminal arms.
About this Structure
1TRR is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.
Reference
Tandem binding in crystals of a trp repressor/operator half-site complex., Lawson CL, Carey J, Nature. 1993 Nov 11;366(6451):178-82. PMID:8232559
Page seeded by OCA on Thu Feb 21 15:16:40 2008
