Structural consequences of two methyl additions in the E. coli trp repressor L-tryptophan binding pocket

Conference · Fri Dec 01 00:00:00 EST 1995

OSTI ID:159351

Lawson, C L

The flexibility and specificity of the L-tryptophan corepressor binding pocket of E coli trp repressor are being investigated by high-resolution crystallographic examination of aporepressor/corepressor analog complexes. While addition of a methyl group on the corepressor indole (5-methyl-tryptophan) results in a small but measurable shift in the position of that functional group introduction of a methyl group on a nearby residue in the binding pocket (Val 58 {yields} Ile) leaves the indole position of L-tryptophan essentially unchanged. Careful alignment of these structures with aporepressor/L-tryptophan/operator-DNA complexes reveal why 5-methyltryptophan is a better corepressor than L-tryptophan.

• Research Organization: Brookhaven National Lab. (BNL), Upton, NY (United States)
• Sponsoring Organization: USDOE, Washington, DC (United States)
• DOE Contract Number: AC02-76CH00016
• OSTI ID: 159351
• Report Number(s): BNL-62320; CONF-9506267-2; ON: DE96002499
• Resource Relation: Conference: 9. conversation in biomolecular stereodynamics, Albany, NY (United States), 20-24 Jun 1995; Other Information: PBD: [1995]
• Country of Publication: United States
• Language: English

Related Subjects

55 BIOLOGY AND MEDICINE
BASIC STUDIES
GENE REPRESSORS
STRUCTURE-ACTIVITY RELATIONSHIPS
PROTEIN STRUCTURE
ESCHERICHIA COLI
TRYPTOPHAN
BIOCHEMICAL REACTION KINETICS
CRYSTALS
X-RAY DIFFRACTION