Flexibility of the DNA-binding domains of trp repressor

C. L. Lawson, R. Zhang, R. W. Schevitz, Z. Otwinowski, A. Joachimiak, P. B. Sigler

Research output: Contribution to journalArticle

123 Citations (Scopus)

Abstract

An orthorhombic crystal form of trp repressor (aporepressor plus L-tryptophan ligand) was solved by molecular replacement, refined to 1.65 99 resolution, and compared to the structure of the repressor in trigonal crystals. Even though these two crystal forms of repressor were grown under identical conditions, the refined structures have distinctly different conformations of the DNA-binding domains. Unlike the repressor/aporepressor structural transition, the conformational shift is not caused by the binding or loss of the L-tryptophan ligand. We conclude that while L-tryptophan binding is essential for forming a specific complex with trp operator DNA, the corepressor ligand does not lock the repressor into a single conformation that is complementary to the operator. This flexibility may be required by the various binding modes proposed for trp repressor in its search for and adherence to its three different operator sites.

Original languageEnglish (US)
Pages (from-to)18-31
Number of pages14
JournalProteins: Structure, Function and Genetics
Volume3
Issue number1
StatePublished - 1988

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Tryptophan
Ligands
Crystals
Conformations
DNA
Nucleic Acid Conformation
Co-Repressor Proteins
E coli TRPR protein

ASJC Scopus subject areas

  • Biochemistry
  • Genetics
  • Structural Biology

Cite this

Lawson, C. L., Zhang, R., Schevitz, R. W., Otwinowski, Z., Joachimiak, A., & Sigler, P. B. (1988). Flexibility of the DNA-binding domains of trp repressor. Proteins: Structure, Function and Genetics, 3(1), 18-31.

Flexibility of the DNA-binding domains of trp repressor. / Lawson, C. L.; Zhang, R.; Schevitz, R. W.; Otwinowski, Z.; Joachimiak, A.; Sigler, P. B.

In: Proteins: Structure, Function and Genetics, Vol. 3, No. 1, 1988, p. 18-31.

Research output: Contribution to journalArticle

Lawson, CL, Zhang, R, Schevitz, RW, Otwinowski, Z, Joachimiak, A & Sigler, PB 1988, 'Flexibility of the DNA-binding domains of trp repressor', Proteins: Structure, Function and Genetics, vol. 3, no. 1, pp. 18-31.
Lawson CL, Zhang R, Schevitz RW, Otwinowski Z, Joachimiak A, Sigler PB. Flexibility of the DNA-binding domains of trp repressor. Proteins: Structure, Function and Genetics. 1988;3(1):18-31.
Lawson, C. L. ; Zhang, R. ; Schevitz, R. W. ; Otwinowski, Z. ; Joachimiak, A. ; Sigler, P. B. / Flexibility of the DNA-binding domains of trp repressor. In: Proteins: Structure, Function and Genetics. 1988 ; Vol. 3, No. 1. pp. 18-31.
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