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2KEK

Solution structure of a dimer of LAC repressor DNA-binding domain complexed to its natural operator O3

Summary for 2KEK
Entry DOI10.2210/pdb2kek/pdb
Related1L1M 2KEI 2KEJ
DescriptorLactose operon repressor, DNA (5'-D(*CP*GP*GP*CP*AP*GP*TP*GP*AP*GP*CP*GP*CP*AP*AP*CP*GP*CP*AP*AP*TP*TP*C)-3'), DNA (5'-D(P*GP*AP*AP*TP*TP*GP*CP*GP*TP*TP*GP*CP*GP*CP*TP*CP*AP*CP*TP*GP*CP*CP*G)-3') (3 entities in total)
Functional Keywordslac repressor, lac operators, protein-dna complex, dna-binding, repressor, transcription, transcription regulation, transcription-dna complex, transcription/dna
Biological sourceEscherichia coli
Total number of polymer chains4
Total formula weight27769.62
Authors
Romanuka, J.,Folkers, G.,Biris, N.,Tishchenko, E.,Wienk, H.,Kaptein, R.,Boelens, R. (deposition date: 2009-01-30, release date: 2009-05-19, Last modification date: 2021-10-20)
Primary citationRomanuka, J.,Folkers, G.E.,Biris, N.,Tishchenko, E.,Wienk, H.,Bonvin, A.M.,Kaptein, R.,Boelens, R.
Specificity and affinity of Lac repressor for the auxiliary operators O2 and O3 are explained by the structures of their protein-DNA complexes.
J.Mol.Biol., 390:478-489, 2009
Cited by
PubMed Abstract: The structures of a dimeric mutant of the Lac repressor DNA-binding domain complexed with the auxiliary operators O2 and O3 have been determined using NMR spectroscopy and compared to the structures of the previously determined Lac-O1 and Lac-nonoperator complexes. Structural analysis of the Lac-O1 and Lac-O2 complexes shows highly similar structures with very similar numbers of specific and nonspecific contacts, in agreement with similar affinities for these two operators. The left monomer of the Lac repressor in the Lac-O3 complex retains most of these specific contacts. However, in the right half-site of the O3 operator, there is a significant loss of protein-DNA contacts, explaining the low affinity of the Lac repressor for the O3 operator. The binding mode in the right half-site resembles that of the nonspecific complex. In contrast to the Lac-nonoperator DNA complex where no hinge helices are formed, the stability of the hinge helices in the weak Lac-O3 complex is the same as in the Lac-O1 and Lac-O2 complexes, as judged from the results of hydrogen/deuterium experiments.
PubMed: 19450607
DOI: 10.1016/j.jmb.2009.05.022
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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