The operator-binding domain of lambda repressor: structure and DNA recognition - PubMed (original) (raw)
. 1982 Jul 29;298(5873):443-7.
doi: 10.1038/298443a0.
- PMID: 7088190
- DOI: 10.1038/298443a0
The operator-binding domain of lambda repressor: structure and DNA recognition
C O Pabo et al. Nature. 1982.
Abstract
The structure of the operator-binding domain of the lambda repressor has been determined at 3.2 A resolution. This domain contains an extended N-terminal arm and five alpha-helices. Model-building studies of the repressor-operator complex suggest that alpha-helices, especially the N-terminal parts of these helices, may provide a useful surface for protein-DNA interactions.
Similar articles
- The N-terminal arms of lambda repressor wrap around the operator DNA.
Pabo CO, Krovatin W, Jeffrey A, Sauer RT. Pabo CO, et al. Nature. 1982 Jul 29;298(5873):441-3. doi: 10.1038/298441a0. Nature. 1982. PMID: 7088189 - Recognition of a DNA operator by the repressor of phage 434: a view at high resolution.
Aggarwal AK, Rodgers DW, Drottar M, Ptashne M, Harrison SC. Aggarwal AK, et al. Science. 1988 Nov 11;242(4880):899-907. doi: 10.1126/science.3187531. Science. 1988. PMID: 3187531 - How lambda repressor and lambda Cro distinguish between OR1 and OR3.
Hochschild A, Douhan J 3rd, Ptashne M. Hochschild A, et al. Cell. 1986 Dec 5;47(5):807-16. doi: 10.1016/0092-8674(86)90523-4. Cell. 1986. PMID: 2946418 - Protein-DNA recognition.
Pabo CO, Sauer RT. Pabo CO, et al. Annu Rev Biochem. 1984;53:293-321. doi: 10.1146/annurev.bi.53.070184.001453. Annu Rev Biochem. 1984. PMID: 6236744 Review. - Comparison of the structures of operator DNA free and in complex with lambda repressor.
Baleja JD, Sykes BD. Baleja JD, et al. Biochem Cell Biol. 1991 Feb-Mar;69(2-3):202-5. doi: 10.1139/o91-030. Biochem Cell Biol. 1991. PMID: 2031722 Review.
Cited by
- Tn10 tet operator mutations affecting Tet repressor recognition.
Wissmann A, Meier I, Wray LV Jr, Geissendörfer M, Hillen W. Wissmann A, et al. Nucleic Acids Res. 1986 May 27;14(10):4253-66. doi: 10.1093/nar/14.10.4253. Nucleic Acids Res. 1986. PMID: 3086838 Free PMC article. - Ribosomal protein L7/L12 has a helix-turn-helix motif similar to that found in DNA-binding regulatory proteins.
Rice PA, Steitz TA. Rice PA, et al. Nucleic Acids Res. 1989 May 25;17(10):3757-62. doi: 10.1093/nar/17.10.3757. Nucleic Acids Res. 1989. PMID: 2660100 Free PMC article. - Overproduction of the cyclic AMP receptor protein of Escherichia coli and expression of the engineered C-terminal DNA-binding domain.
Gronenborn AM, Clore GM. Gronenborn AM, et al. Biochem J. 1986 Jun 15;236(3):643-9. doi: 10.1042/bj2360643. Biochem J. 1986. PMID: 3539103 Free PMC article. - The C-terminal domain of the Escherichia coli RNA polymerase alpha subunit plays a role in the CI-dependent activation of the bacteriophage lambda pM promoter.
Kedzierska B, Szambowska A, Herman-Antosiewicz A, Lee DJ, Busby SJ, Wegrzyn G, Thomas MS. Kedzierska B, et al. Nucleic Acids Res. 2007;35(7):2311-20. doi: 10.1093/nar/gkm123. Epub 2007 Mar 27. Nucleic Acids Res. 2007. PMID: 17389649 Free PMC article. - The possible roles of residues 79 and 80 of the Trp repressor from Escherichia coli K-12 in trp operator recognition.
Güneş C, Staacke D, von Wilcken-Bergmann B, Müller-Hill B. Güneş C, et al. Mol Gen Genet. 1995 Jan 20;246(2):180-95. doi: 10.1007/BF00294681. Mol Gen Genet. 1995. PMID: 7862089
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources