Crystallization and structure solution at 4 A resolution of the recombinant synthase domain of N(5'-phosphoribosyl)anthranilate isomerase:indole-3-glycerol-phosphate synthase from Escherichia coli complexed to a substrate analogue |
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Authors: | Wilmanns, Matthias Schlagenhauf, Edith Fol, Bruno Jansonius, Johan N |
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Affiliation: | Department of Structural Biology, Biocentre, University of Basel Klingelbergstrasse 70, CH-4056 Basel, Switzerland |
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Abstract: | The recombinant synthase domain of the bifunctional enzyme N-(5'-phosphoribosyl)anthranilateisomerase:indole-3-glycerol-phosphate synthase from Escherichiacoli has been crystallized, and the structure has been solvedat 4 Å resolution. Two closely related crystal forms grownfrom ammonium sulphate diffract to 2 Å resolution. Oneform (space group R32, a = 163 Å, = 29.5°) containsthe unliganded synthase domain; the second crystal form (spacegroup P6322, a = 144 Å, c = 158 Å) is co-crystallizedwith the substrate analogue N-(5'-phosphoribit-1-yl)anthranilate.The structure of the synthaseinhibitor complex has beensolved by the molecular replacement method. This achievementrepresents the first successful use of a (ß)g-barrelmonomer as a trial model. The recombinant synthase domain associatesas a trimer in the crystal, the molecules being related by apseudo-crystallographic triad. The interface contacts betweenthe three domains are mediated by those residues that are alsoinvolved in the domain interface of the bifunctional enzyme.This system provides a model for an interface which is usedin both intermolecular and intramolecular domain contacts. |
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Keywords: | (ß /math/alpha.gif" ALT=" {alpha}" BORDER=" 0" >)8-barrel/ crystal structure/ IGP synthase/ interface contacts/ molecular replacement |
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