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show all sequences of 2.7.7.62

Solution structural studies of GTP:adenosylcobinamide-phosphateguanylyl transferase (CobY) from Methanocaldococcus jannaschii

Singarapu, K.K.; Otte, M.M.; Tonelli, M.; Westler, W.M.; Escalante-Semerena, J.C.; Markley, J.L.; PLoS ONE 10, e0141297 (2015)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
the solution structure has a mixed alpha/beta fold consisting of seven beta-strands and five alpha-helices, very similar to a Rossmann fold. Titration of apo-CobY with GTP results in large changes in amide proton chemical shifts. The CobY:GTP complex is unstable over time, GTP hydrolyzes and the protein converts slowly to a species with an NMR spectrum similar to that of apo-CobY. The variant CobYG153D, yields NMR spectra similar to those of wild-type CobY in both its apo-state and in complex with GTP. The CobYG153D:GTP complex is also unstable over time
Methanocaldococcus jannaschii
Engineering
Amino acid exchange
Commentary
Organism
G153D
residues R13 and K19 of the mutant directly coordinate the phosphate group of GTP in the X-ray structure. The X-ray structure of the CobYG153D:GTP complex is modeled as a homodimer
Methanocaldococcus jannaschii
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Methanocaldococcus jannaschii
Q58517
-
-
Methanocaldococcus jannaschii DSM 2661
Q58517
-
-
Subunits
Subunits
Commentary
Organism
monomer
wild-type CobY is monomeric in solution in both its apo- and GTP-bound formssolution structural studies
Methanocaldococcus jannaschii
Crystallization (Commentary) (protein specific)
Crystallization
Organism
the solution structure has a mixed alpha/beta fold consisting of seven beta-strands and five alpha-helices, very similar to a Rossmann fold. Titration of apo-CobY with GTP results in large changes in amide proton chemical shifts. The CobY:GTP complex is unstable over time, GTP hydrolyzes and the protein converts slowly to a species with an NMR spectrum similar to that of apo-CobY. The variant CobYG153D, yields NMR spectra similar to those of wild-type CobY in both its apo-state and in complex with GTP. The CobYG153D:GTP complex is also unstable over time
Methanocaldococcus jannaschii
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
G153D
residues R13 and K19 of the mutant directly coordinate the phosphate group of GTP in the X-ray structure. The X-ray structure of the CobYG153D:GTP complex is modeled as a homodimer
Methanocaldococcus jannaschii
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
wild-type CobY is monomeric in solution in both its apo- and GTP-bound formssolution structural studies
Methanocaldococcus jannaschii
Other publictions for EC 2.7.7.62
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)
739433
Singarapu
Solution structural studies of ...
Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661
PLoS ONE
10
e0141297
2015
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5301-5313
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702316
Otte
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Methanocaldococcus jannaschii
Biochemistry
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5882-5889
2009
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694244
Gray
The genome of Rhodobacter spha ...
Rhodobacter sphaeroides
Mol. Microbiol.
70
824-836
2008
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674340
Otte
The thiamine kinase (YcfN) enz ...
Escherichia coli, Salmonella enterica
J. Bacteriol.
189
7310-7315
2007
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663316
Hsu
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Protein Expr. Purif.
42
178-181
2005
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644278
Warren
The biosynthesis of adenosylco ...
Bacillus megaterium, Escherichia coli, Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus DELTAH, Propionibacterium freudenreichii, Pseudomonas denitrificans (nomen rejiciendum), Salmonella enterica
Nat. Prod. Rep.
19
390-412
2002
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1
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644438
Thomas
Analysis of the adenosylcobina ...
Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium LT2
J. Biol. Chem.
275
27576-27586
2000
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644437
Thompson
Three-dimensional structure of ...
Salmonella enterica subsp. enterica serovar Typhimurium
Biochemistry
38
12995-13005
1999
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644436
Thompson
Three-dimensional structure of ...
Salmonella enterica subsp. enterica serovar Typhimurium
Biochemistry
37
7686-7695
1998
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644435
O'Toole
Purification and characterizat ...
Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium LT2
J. Biol. Chem.
270
23560-23569
1995
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651620
O'Toole
cobU-dependent assimilation of ...
Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium LT2
J. Bacteriol.
175
6328-6336
1993
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