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2WJZ
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CRYSTAL STRUCTURE OF (HISH) K181A Y138A MUTANT OF IMIDAZOLEGLYCEROLPHOSPHATE SYNTHASE (HISH HISF) WHICH DISPLAYS CONSTITUTIVE GLUTAMINASE ACTIVITY
Descriptor:IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE HISF, IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISH, PHOSPHATE ION
Authors:Vega, M.C., List, F., Razeto, A., Haeger, M.C., Babinger, K., Kuper, J., Sterner, R., Wilmanns, M.
Deposit date:2009-06-02
Release date:2010-08-25
Last modified:2013-01-09
Method:X-RAY DIFFRACTION (2.601 Å)
Cite:Catalysis Uncoupling in a Glutamine Amidotransferase Bienzyme by Unblocking the Glutaminase Active Site.
Chem.Biol., 19, 2012
3OG3
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CRYSTAL STRUCTURE OF AN ARTIFICIAL THERMOSTABLE (BA)8-BARREL PROTEIN FROM IDENTICAL HALF BARRELS
Descriptor:Imidazole glycerol phosphate synthase subunit hisF, SULFATE ION, CHLORIDE ION
Authors:Sperl, J.M., Bocola, M., List, F., Kellerer, B., Sterner, R.
Deposit date:2010-08-16
Release date:2011-08-17
Last modified:2017-08-09
Method:X-RAY DIFFRACTION (2.08 Å)
Cite:Design of an artificial thermostable (BA)8-barrel protein from identical half barrels
To be Published
4EWN
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STRUCTURE OF HISF-D130V+D176V WITH BOUND RCDRP
Descriptor:Imidazole glycerol phosphate synthase subunit HisF, 1-(O-carboxy-phenylamino)-1-deoxy-D-ribulose-5-phosphate
Authors:Reisinger, B., Bocola, M., Rajendran, C., List, F., Sterner, R.
Deposit date:2012-04-27
Release date:2012-12-05
Method:X-RAY DIFFRACTION (1.903 Å)
Cite:A sugar isomerization reaction established on various (beta-alpha)8-barrel scaffolds is based on substrate-assisted catalysis
Protein Eng.Des.Sel., 25, 2012
3ZR4
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STRUCTURAL EVIDENCE FOR AMMONIA TUNNELING ACROSS THE (BETA-ALPHA)8 BARREL OF THE IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE BIENZYME COMPLEX
Descriptor:IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISF, IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISH, GLYCEROL, ...
Authors:Vega, M.C., Kuper, J., Haeger, M.C., Mohrlueder, J., Marquardt, S., Sterner, R., Wilmanns, M.
Deposit date:2011-06-13
Release date:2012-10-03
Last modified:2013-01-09
Method:X-RAY DIFFRACTION (2.41 Å)
Cite:Catalysis Uncoupling in a Glutamine Amidotransferase Bienzyme by Unblocking the Glutaminase Active Site.
Chem.Biol., 19, 2012