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2BJC

NMR structure of a protein-DNA complex of an altered specificity mutant of the lac repressor headpiece that mimics the gal repressor

Summary for 2BJC
Entry DOI10.2210/pdb2bjc/pdb
Related1CJG 1EFA 1JWL 1JYE 1JYF 1L1M 1LBG 1LBH 1LBI 1LCC 1LCD 1LQC 1LTP 1OSL 1TLF
NMR InformationBMRB: 7354
DescriptorLACTOSE OPERON REPRESSOR, 5'-D(*GP*AP*AP*TP*TP*GP*TP*AP*AP*GP *CP*GP*CP*TP*TP*AP*CP*AP*AP*TP*TP*C)-3' (2 entities in total)
Functional Keywordstranscription regulator, symmetric dna-binding, dna-binding, hth, lac operon, lac repressor, altered specificity, mutant, repressor, transcription regulation, transcription regulator/dna, gal repressor, gal operon, lac headpiece, symmetric dimer
Biological sourceESCHERICHIA COLI
Total number of polymer chains4
Total formula weight26904.10
Authors
Salinas, R.K.,Folkers, G.E.,Bonvin, A.M.J.J.,Das, D.,Boelens, R.,Kaptein, R. (deposition date: 2005-02-01, release date: 2005-10-18, Last modification date: 2024-11-20)
Primary citationSalinas, R.K.,Folkers, G.E.,Bonvin, A.M.J.J.,Das, D.,Boelens, R.,Kaptein, R.
Altered Specificity in DNA Binding by the Lac Repressor: A Mutant Lac Headpiece that Mimics the Gal Repressor
Chembiochem, 6:1628-, 2005
Cited by
PubMed Abstract: Recognition of the lac operator by the lac repressor involves specific interactions between residues in the repressor's recognition helix and bases in the DNA major groove. Tyr17 and Gln18, at positions 1 and 2 in the lac repressor recognition helix, can be exchanged for other amino acids to generate mutant repressors that display altered specificity. We have solved the solution structure of a protein-DNA complex of an altered-specificity mutant lac headpiece in which Tyr17 and Gln18 were exchanged for valine and alanine, respectively, as found in the recognition helix of the gal repressor. As previously described by Lehming et al. (EMBO J. 1987, 6, 3145-3153), this altered-specificity mutant of the lac repressor recognizes a variant lac operator that is similar to the gal operator Oe. The mutant lac headpiece showed the predicted specificity and is also able to mimic the gal repressor by recognizing and bending the natural gal operator Oe. These structural data show that, while most of the anchoring points that help the lac headpiece to assemble on the lac operator were preserved, a different network of protein-DNA interactions connecting Ala17 and Val18 to bases in the DNA major groove drives the specificity towards the altered operator.
PubMed: 16094693
DOI: 10.1002/CBIC.200500049
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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