1trr
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(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...)
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Revision as of 01:25, 21 November 2007
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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 TRP 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
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