1TRR

TANDEM BINDING IN CRYSTALS OF A TRP REPRESSOR/OPERATOR HALF-SITE COMPLEX

Summary for 1TRR

• Entry DOI: 10.2210/pdb1trr/pdb
• Descriptor: DNA (5'-D(*AP*GP*CP*GP*TP*AP*CP*TP*AP*GP*TP*AP*CP*GP*CP*T)-3'), PROTEIN (TRP REPRESSOR), TRYPTOPHAN, ... (4 entities in total)
• Functional Keywords: protein-dna complex, transcription-dna complex, transcription/dna
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A881
• Total number of polymer chains: 12
• Total formula weight: 119145.92

Authors

Lawson, C.L.,Carey, J. (deposition date: 1993-10-21, release date: 1993-10-21, Last modification date: 2024-02-14)

Primary citation

Lawson, C.L.,Carey, J.
Tandem binding in crystals of a trp repressor/operator half-site complex.
Nature, 366:178-182, 1993

PubMed Abstract: 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.

PubMed: 8232559
DOI: 10.1038/366178a0

Experimental method

X-RAY DIFFRACTION (2.4 Å)