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spinqualitylabelsall models 2c3z, resolution 2.8Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF A TRUNCATED VARIANT OF INDOLE-3-GLYCEROL PHOSPHATE SYNTHASE FROM SULFOLOBUS SOLFATARICUS

Overview

Indole-3-glycerol phosphate synthase (IGPS) catalyzes the fifth step in, the biosynthesis of tryptophan. It belongs to the large and versatile, family of (betaalpha)(8)-barrel enzymes but has an unusual N-terminal, extension of about 40 residues. Limited proteolysis with trypsin of IGPS, from both Sulfolobus solfataricus (sIGPS) and Thermotoga maritima (tIGPS), removes about 25 N-terminal residues and one of the two extra helices, contained therein. To assess the role of the extension, the N-terminally, truncated variants sIGPSDelta(1-26) and tIGPSDelta(1-25) were produced, recombinantly in Escherichia coli, purified, and characterized in, comparison to the wild-type enzymes. Both sIGPSDelta(1-26) and, tIGPSDelta(1-25) have unchanged oligomerization states and turnover, numbers. In ... [(full description)]

About this Structure

2C3Z is a [Single protein] structure of sequence from [Sulfolobus solfataricus] with SO4 as [ligand]. Active as [[1]], with EC number [4.1.1.48]. Full crystallographic information is available from [OCA].

Reference

Role of the N-terminal extension of the (betaalpha)8-barrel enzyme indole-3-glycerol phosphate synthase for its fold, stability, and catalytic activity., Schneider B, Knochel T, Darimont B, Hennig M, Dietrich S, Babinger K, Kirschner K, Sterner R, Biochemistry. 2005 Dec 20;44(50):16405-12. PMID:16342933

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