+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

Structures of wild-type and P28L/Y173F tryptophan synthase alpha-subunits from Escherichia coli



Structures of wild-type and P28L/Y173F tryptophan synthase alpha-subunits from Escherichia coli



Biochemical and Biophysical Research Communications 323(4): 1257-1264



The alpha-subunit of tryptophan synthase (alphaTS) catalyzes the cleavage of indole-3-glycerol phosphate to glyceraldehyde-3-phosphate and indole, which is used to yield the amino acid tryptophan in tryptophan biosynthesis. Here, we report the first crystal structures of wild-type and double-mutant P28L/Y173F alpha-subunit of tryptophan synthase from Escherichia coli at 2.8 and 1.8 ANG resolution, respectively.

Please choose payment method:






(PDF emailed within 0-6 h: $19.90)

Accession: 012592516

Download citation: RISBibTeXText

PMID: 15451433

DOI: 10.1016/j.bbrc.2004.08.222


Related references

Crystallization and X-ray crystallographic studies of wild-type and mutant tryptophan synthase alpha-subunits from Escherichia coli. Molecules and Cells 19(2): 219-222, 2005

Immunochemical comparisons of mutant and wild type alpha subunits of enz tryptophan synthetase escherichia coli. Archives of Biochemistry & Biophysics 127(1/2/3): 7-16, 1968

Unfolding properties of tryptophan-containing alpha-subunits of the Escherichia coli tryptophan synthase. Journal of Biological Chemistry 270(47): 28177-28182, 1995

Tryptophan-containing alpha-subunits of the Escherichia coli tryptophan synthase. Enzymatic and urea stability properties. Journal of Biological Chemistry 270(30): 17712-5, 1995

Subunit interaction in tryptophan synthase ec 4.2.1.20 of escherichia coli calorimetric studies on association of alpha subunits and beta 2 subunits. Biochemistry 18(10): 1979-1984, 1979

Influence of alpha-subunits on the high-pressure stability of apo and holo beta-2-subunits in the bienzyme complex tryptophan synthase from Escherichia coli. Biochemistry. 34(6): -1967, 1995

Substrate interactions with the alpha-subunit of the Escherichia coli tryptophan synthase. A kinetic study of the wild-type alpha-subunit. Archives of Biochemistry and Biophysics 181(2): 419-427, 1977

Comparison of denaturation by guanidine hydrochloride of the wild type tryptophan synthase alpha-subunit of Escherichia coli and two mutant protein (Glu 49 replaced by Met or Gln). Journal of Biochemistry 85(4): 915-921, 1979

Homodimers of mutant tryptophan synthase alpha-subunits in Escherichia coli. Biochemical and Biophysical Research Communications 289(2): 568-572, 2001

Substrate interactions with the alpha-subunit of the Escherichia coli tryptophan synthase. A study of the activity of mutant alpha-subunits. Archives of Biochemistry and Biophysics 181(2): 428-437, 1977

Thermal stabilities of mutant Escherichia coli tryptophan synthase alpha subunits. Archives of Biochemistry and Biophysics 292(1): 34-41, 1992

Enzymatic properties of mutant Escherichia coli tryptophan synthase alpha-subunits. Journal of Biological Chemistry 266(30): 20205-20212, 1991

Crystallization and preliminary X-ray analysis of tryptophan synthase alpha-subunits from Escherichia coli. Acta Crystallographica. Section D Biological Crystallography 60(Pt 1): 132-134, 2004

Structure and folding of mutant escherichia coli tryptophan synthase alpha subunits. Journal of Cellular Biochemistry Suppl. (9 Part B): 95, 1985