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Direct and indirect readout in mutant Met repressor-operator complexes
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title
Direct and indirect readout in mutant Met repressor-operator complexes
(English)
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author name string
C W Garvie
series ordinal
1
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S E Phillips
series ordinal
2
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publication date
15 September 2000
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published in
Structure
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volume
8
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issue
9
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page(s)
905-14
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cites work
Regulation of methionine biosynthesis in the enterobacteriaceae
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Cooperative tandem binding of met repressor of Escherichia coli
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Electrostatic activation of Escherichia coli methionine repressor
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Probing the molecular mechanism of action of co-repressor in the E. coli methionine repressor-operator complex using surface plasmon resonance (SPR).
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Evolution in biosynthetic pathways: two enzymes catalyzing consecutive steps in methionine biosynthesis originate from a common ancestor and possess a similar regulatory region
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Three-dimensional crystal structures of Escherichia coli met repressor with and without corepressor
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Crystal structure of the met repressor-operator complex at 2.8 A resolution reveals DNA recognition by beta-strands
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The alpha-helix dipole and the properties of proteins
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DNA recognition by beta-sheets in the Arc repressor-operator crystal structure
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DNA recognition by proteins with the helix-turn-helix motif
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A hypothesis on a specific sequence-dependent conformation of DNA and its relation to the binding of the lac-repressor protein
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Effects of systematic variation of the minimal Escherichia coli met consensus operator site: in vivo and in vitromet repressor binding
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In vitro evolution of the DNA binding sites of Escherichia coli methionine repressor, MetJ.
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Structure and function of Escherichia coli met repressor: similarities and contrasts with trp repressor
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Determinants of repressor/operator recognition from the structure of the trp operator binding site.
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Structural comparison between the d(CTAG) sequence in oligonucleotides and trp and met repressor-operator complexes
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Crystal structure of trp repressor/operator complex at atomic resolution
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Structure of a B-DNA decamer with a central T-A step: C-G-A-T-T-A-A-T-C-G
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The CCP4 suite: programs for protein crystallography
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Diffraction methods for biological macromolecules. Interactive computer graphics: FRODO
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Free R value: a novel statistical quantity for assessing the accuracy of crystal structures
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PROCHECK: a program to check the stereochemical quality of protein structures
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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
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Raster3D Version 2.0. A program for photorealistic molecular graphics
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Identifiers
DOI
10.1016/S0969-2126(00)00182-9
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PubMed publication ID
10986458
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