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show all sequences of 4.3.1.B2

Crystal structure of imidazole glycerol phosphate synthase: a tunnel through a (beta/alpha)8 barrel joins two active sites

Chaudhuri, B.N.; Lange, S.C.; Myers, R.S.; Chittur, S.V.; Davisson, V.J.; Smith, J.L.; Structure 9, 987-997 (2001)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
crystallization at 20°C by hanging-drop vapor diffusion from a 1:1 mixture of protein solution and reservoir solution [22%–28% polyethylene glycol MME 5000, 0.1 M MES (pH 6.5–7.0), and 0.2 M (NH4)2SO4]. Crystals grow in 7–10 days to an average size of 0.12 * 0.12 * 0.08 mM. The 2.1 A crystal structure of imidazole glycerol phosphate synthase reveals extensive interaction of the glutaminase and cyclase catalytic domains. At the domain interface, the glutaminase active site points into the bottomof the (beta/alpha)8 barrel of the cyclase domain. An ammonia tunnel through the (beta/alpha)8 barrel connects the glutaminase docking site at the bottom to the cyclase active site at the top. A conserved gate of four charged residues controls access to the tunnel
Saccharomyces cerevisiae
Inhibitors
Inhibitors
Commentary
Organism
Structure
acivicin
-
Saccharomyces cerevisiae
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Saccharomyces cerevisiae
P33734
-
-
Purification (Commentary)
Commentary
Organism
-
Saccharomyces cerevisiae
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
-
728818
Saccharomyces cerevisiae
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
NH4+ + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
-
728818
Saccharomyces cerevisiae
D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
Crystallization (Commentary) (protein specific)
Crystallization
Organism
crystallization at 20°C by hanging-drop vapor diffusion from a 1:1 mixture of protein solution and reservoir solution [22%–28% polyethylene glycol MME 5000, 0.1 M MES (pH 6.5–7.0), and 0.2 M (NH4)2SO4]. Crystals grow in 7–10 days to an average size of 0.12 * 0.12 * 0.08 mM. The 2.1 A crystal structure of imidazole glycerol phosphate synthase reveals extensive interaction of the glutaminase and cyclase catalytic domains. At the domain interface, the glutaminase active site points into the bottomof the (beta/alpha)8 barrel of the cyclase domain. An ammonia tunnel through the (beta/alpha)8 barrel connects the glutaminase docking site at the bottom to the cyclase active site at the top. A conserved gate of four charged residues controls access to the tunnel
Saccharomyces cerevisiae
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
acivicin
-
Saccharomyces cerevisiae
Purification (Commentary) (protein specific)
Commentary
Organism
-
Saccharomyces cerevisiae
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
-
728818
Saccharomyces cerevisiae
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
NH4+ + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
-
728818
Saccharomyces cerevisiae
D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
Other publictions for EC 4.3.1.B2
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
728756
Liebold
The interaction of ammonia and ...
Thermotoga maritima
Protein Sci.
19
1774-1782
2010
-
-
1
-
1
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4
-
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-
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3
-
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1
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1
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2
1
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1
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1
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4
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1
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2
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1
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2
1
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-
726941
Myers
Reaction coupling through inte ...
Saccharomyces cerevisiae
Biochemistry
44
11974-11985
2005
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-
-
-
5
-
-
18
-
-
-
-
-
1
-
-
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-
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3
-
1
-
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18
1
-
-
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-
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5
-
-
-
-
18
-
-
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-
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-
3
-
1
-
-
18
1
-
-
-
-
-
-
-
18
18
727051
Demin
Kinetic model of imidazologlyc ...
Escherichia coli
Biochemistry
69
1324-1335
2004
-
-
-
-
-
-
-
1
-
-
-
-
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1
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1
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1
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1
-
-
-
-
-
-
-
-
1
1
726938
Chaudhuri
Toward understanding the mecha ...
Saccharomyces cerevisiae
Biochemistry
42
7003-7012
2003
-
-
-
1
-
-
2
-
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1
-
1
-
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3
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1
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2
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1
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3
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-
726939
Myers
Substrate-induced changes in t ...
Saccharomyces cerevisiae
Biochemistry
42
7013-7022
2003
-
-
-
-
7
-
3
22
-
-
-
-
-
3
-
-
1
-
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-
3
-
1
-
-
22
1
-
-
-
7
-
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7
-
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3
7
22
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1
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3
-
1
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22
1
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-
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24
24
727791
Omi
Structure of imidazole glycero ...
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
J. Biochem.
132
759-765
2002
-
-
-
1
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2
-
93
-
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4
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4
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1
1
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728807
Douangamath
Structural evidence for ammoni ...
Thermotoga maritima, Thermotoga maritima DSM 3109
Structure
10
185-193
2002
-
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1
-
-
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-
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4
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1
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2
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1
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2
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1
1
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727736
Klem
-
Subunit interactions and gluta ...
Escherichia coli
J. Bacteriol.
182
989-996
2001
-
-
1
-
4
-
-
10
-
-
-
1
-
1
-
-
1
-
-
-
-
-
2
1
1
-
-
8
1
-
-
-
-
-
-
-
-
1
-
-
4
-
-
-
-
10
-
-
-
1
-
-
-
1
-
-
-
-
2
1
1
-
-
8
1
-
-
-
-
-
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-
9
9
728818
Chaudhuri
Crystal structure of imidazole ...
Saccharomyces cerevisiae
Structure
9
987-997
2001
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1
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1
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3
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1
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748148
Beismann-Driemeyer
Imidazole glycerol phosphate ...
Thermotoga maritima, Thermotoga maritima DSM 3109
J. Biol. Chem.
276
20387-20396
2001
-
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1
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9
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2
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6
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1
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6
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1
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1
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1
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9
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2
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1
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6
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1
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2
1
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1
1
-
2
2
728731
Chittur
Expression and purification of ...
Saccharomyces cerevisiae
Protein Expr. Purif.
18
366-377
2000
-
-
1
-
-
-
-
2
-
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3
1
-
3
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1
-
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1
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3
1
1
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2
1
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1
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1
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1
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1
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3
1
1
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2
1
-
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-
1
1
-
2
2
726928
Klem
Imidazole glycerol phosphate s ...
Escherichia coli
Biochemistry
32
5177-5186
1993
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1
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2
7
-
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5
1
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2
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1
3
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1
4
1
1
-
1
6
3
2
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1
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2
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7
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5
1
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1
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1
4
1
1
-
1
6
3
2
-
-
-
-
-
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7
7