1beu: Difference between revisions
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[[Category: mutation d60n in a-subunit]] | [[Category: mutation d60n in a-subunit]] | ||
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Revision as of 15:49, 30 October 2007
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TRP SYNTHASE (D60N-IPP-SER) WITH K+
OverviewOverview
We have investigated the role of Asp60 of the alpha-subunit in allosteric, communication between the tryptophan synthase alpha- and beta-subunits., Crystallographic and microspectrophotometric studies have been carried out, on a mutant (alpha D60N) tryptophan synthase alpha 2 beta 2 complex which, has no observable alpha-activity, but has substantial beta-activity., Single-crystal polarized absorption spectra indicate that the external, aldimine is the predominant L-serine intermediate and that the amount of, the intermediate formed is independent of pH, monovalent cations, and, allosteric effectors. The three-dimensional structure is reported for this, mutant enzyme complexed with indole 3-propanol phosphate bound to the, alpha-site and L-serine bound to the beta-site (alpha ... [(full description)]
About this StructureAbout this Structure
1BEU is a [Protein complex] structure of sequences from [Salmonella typhimurium] with K, IPL and PLS as [ligands]. Active as [Tryptophan synthase], with EC number [4.2.1.20]. Structure known Active Sites: NUA and NUB. Full crystallographic information is available from [OCA].
ReferenceReference
Cryocrystallography and microspectrophotometry of a mutant (alpha D60N) tryptophan synthase alpha 2 beta 2 complex reveals allosteric roles of alpha Asp60., Rhee S, Miles EW, Mozzarelli A, Davies DR, Biochemistry. 1998 Jul 28;37(30):10653-9. PMID:9692955
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