Three-dimensional structure of the bifunctional enzyme N-(5'-phosphoribosyl)anthranilate isomerase-indole-3-glycerol-phosphate synthase from Escherichia coli.
- 1 August 1987
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 84 (16) , 5690-5694
- https://doi.org/10.1073/pnas.84.16.5690
Abstract
N-(5''-Phosphoribosyl)anthranilate isomerase-indole-3-glycerol-phosphate synthase from Escherichia coli is a monomeric bifunctional enzyme of Mr 49,500 that catalyzes two sequential reactions in the biosynthesis of tryptophan. The three-dimensional structure of the enzyme has been determined at 2.8-.ANG. resolution by x-ray crystallography. The two catalytic activities reside on distinct functional domains of similar folding, that of an eightfold parallel .beta.-barrel with .alpha.-helices on the outside connecting the .beta.-strands. Both active sites were located with an iodinated substrate analogue and found to be in depressions on the surface of the domains created by the outward-curving loops between the carboxyl termini of the .beta.-sheet strands and the subsequent .alpha.-helices. They do not face each other, making "channeling" of the substrate between active sites virtually impossible. Despite the structural similarity of the two domains, no significant seqeunce homology was found when topologically equivalent residues were compared.This publication has 44 references indexed in Scilit:
- Crystal structure of muconate lactonizing enzyme at 3 Å resolutionJournal of Molecular Biology, 1987
- Nucleotide sequence of the trpD and trpC genes of salmonella typhimuriumJournal of Molecular Biology, 1983
- Structure of 2-keto-3-deoxy-6-phosphogluconate aldolase at 2.8 Å resolutionJournal of Molecular Biology, 1982
- Repeated seeding technique for growing large single crystals of proteinsJournal of Molecular Biology, 1981
- Limited proteolysis of N-(5′-phosphoribosyl)anthranilate isomerase: Indoleglycerol phosphate synthase from Escherichia coli yields two different enzymically active, functional domainsJournal of Molecular Biology, 1980
- Structure of glycolate oxidase from spinach at a resolution of 5.5 ÅJournal of Molecular Biology, 1980
- N-(5-Phosphoribosyl)anthranilate isomerase-indoleglycerol-phosphate synthase. 2. Fast-reaction studies show that a fluorescent substrate analog binds independently to two different sitesBiochemistry, 1979
- Crystal structure of cat muscle pyruvate kinase at a resolution of 2.6 ÅJournal of Molecular Biology, 1979
- The three-dimensional structure of mitochondrial aspartate aminotransferase at 4.5 Å resolutionJournal of Molecular Biology, 1979
- Enzymes of the tryptophan operon of BacillussubtilisBiochemical and Biophysical Research Communications, 1969