(Q27639134)

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The catalytic mechanism of indole-3-glycerol phosphate synthase: crystal structures of complexes of the enzyme from Sulfolobus solfataricus with substrate analogue, substrate, and product

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scholarly article

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The catalytic mechanism of indole-3-glycerol phosphate synthase: crystal structures of complexes of the enzyme from Sulfolobus solfataricus with substrate analogue, substrate, and product (English)

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crystal structure

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Sulfolobus solfataricus

object named as

Sulfolobus solfataricus

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based on heuristic

inferred from title

author name string

Michael Hennig

1

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B D Darimont

2

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J N Jansonius

3

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K Kirschner

4

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language of work or name

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publication date

7 June 2002

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Journal of Molecular Biology

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319

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3

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757-66

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On the conversion of anthranilic acid to indole

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Three-dimensional structure of the bifunctional enzyme N-(5'-phosphoribosyl)anthranilate isomerase-indole-3-glycerol-phosphate synthase from Escherichia coli

1 reference

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Three-dimensional structure of the bifunctional enzyme phosphoribosylanthranilate isomerase: Indoleglycerolphosphate synthase from Escherichia coli refined at 2.0 Å resolution

1 reference

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2.0 A structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: possible determinants of protein stability

1 reference

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The crystal structure of indole-3-glycerol phosphate synthase from the hyperthermophilic archaeon Sulfolobus solfataricus in three different crystal forms: effects of ionic strength

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Indoleglycerol phosphate synthase-phosphoribosyl anthranilate isomerase: comparison of the bifunctional enzyme from Escherichia coli with engineered monofunctional domains

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Mutational analysis of the active site of indoleglycerol phosphate synthase from Escherichia coli

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Indole-3-glycerol-phosphate synthase from Sulfolobus solfataricus as a model for studying thermostable TIM-barrel enzymes.

1 reference

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Improving the catalytic activity of a thermophilic enzyme at low temperatures

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N-(5-Phosphoribosyl)anthranilate isomerase-indoleglycerol-phosphate synthase. 1. A substrate analog binds to two different binding sites on the bifunctional enzyme from Escherichia coli

1 reference

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N-(5-Phosphoribosyl)anthranilate isomerase-indoleglycerol-phosphate synthase. 2. Fast-reaction studies show that a fluorescent substrate analog binds independently to two different sites

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Modification of a catalytically important residue of indoleglycerol-phosphate synthase from Escherichia coli

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Deletion mutagenesis as a test of evolutionary relatedness of indoleglycerol phosphate synthase with other TIM barrel enzymes.

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Phosphoribosyl anthranilate isomerase from Thermotoga maritima is an extremely stable and active homodimer.

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Crystal structure at 2.0 A resolution of phosphoribosyl anthranilate isomerase from the hyperthermophile Thermotoga maritima: possible determinants of protein stability

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Phosphoribosyl anthranilate isomerase catalyzes a reversible amadori reaction.

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The CCP4 suite: programs for protein crystallography

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Phosphoribosylanthranilate isomerase-indoleglycerol-phosphate synthase from Escherichia coli

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Accurate bond and angle parameters for X-ray protein structure refinement

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Improved methods for building protein models in electron density maps and the location of errors in these models

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Improved Fourier coefficients for maps using phases from partial structures with errors

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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

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10.1016/S0022-2836(02)00378-9

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