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dimer or tetramer
isoform SHMT2, X-ray crystallography
monomer
the apo-L276A and the apo-L85A mutants are in the monomeric state
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x * 70000, SDS-PAGE
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x * 70000, SDS-PAGE
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x * 45200, about, sequence calculation, recombinant enzyme, SDS-PAGE
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x * 50000, SDS-PAGE
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x * 45000, SDS-PAGE
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x * 47300, calculated from amino acid sequence
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x * 45400, SDS-PAGE and calculated from amino acid sequence
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x * 50000, SDS-PAGE
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x * 49800, recombinant His-tagged PfSHMTc, SDS-PAGE
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x * 44500, about, sequence calculation, x * 60000, recombinant GST-tagged enzyme, SDS-PAGE
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x * 44500, about, sequence calculation, x * 60000, recombinant GST-tagged enzyme, SDS-PAGE
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x * 45300, recombinant GST-tagged enzyme, SDS-PAGE
dimer
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dimer
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homology modeling and comparison to SHMT from Bacillus stearothermophilus, using the crystal structure, PDB ID 1KKJ, overview
dimer
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview
dimer
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview
dimer
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analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview
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dimer
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview
dimer
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analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview
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dimer
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2 * 46000, SDS-PAGE
dimer
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2 * 47000, calculated from DNA-sequence
dimer
in the 0.0025-0.025 mM subunit concentration range, the wild type SHMT is a dimer, either in the presence or absence of cofactor. The apo-L85A mutant enzyme is approximately 75% dimeric
dimer
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wild-type eSHMT is a dimer in both apo- and holo-enzyme forms
dimer
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview
dimer
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2 * 45000, SDS-PAGE
dimer
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2 * 44000, SDS-PAGE
dimer
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2 * 45000, SDS-PAGE
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dimer
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2 * 44000, SDS-PAGE
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dimer
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gel filtration, crystallographic symmetry
dimer
x-ray crystallography
dimer
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homology modeling using the crystal structure, PDB ID 1KKJ, and comparison to SHMT from Bacillus subtilis, overview
dimer
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview
dimer
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2 * 48000, SDS-PAGE
dimer
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2 * 48200, SDS-PAGE
dimer
2 * 45000, SHM1, SDS-PAGE
dimer
2 * 45500, SHM2, SDS-PAGE
dimer
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview
dimer
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2 * 45500, SHM2, SDS-PAGE
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dimer
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2 * 45000, SHM1, SDS-PAGE
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dimer
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analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview
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dimer
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removal of the bound pyridoxal 5'-phosphate from the mutant tetrameric enzyme leads to dissociation to a dimer
dimer
predicted to be a dimer
dimer
2 * 45050, recombinant N-terminally His-tagged enzyme, mass spectrometry
dimer
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview
dimer
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analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview
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dimer
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview
dimer
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analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview
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dimer
2 * 53000, SDS-PAGE
dimer
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2 * 53000, SDS-PAGE
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dimer
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview
dimer
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview
dimer
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analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview
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dimer
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview
homodimer
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homodimer
2 * 45000, SDS-PAGE
homodimer
2 * 46776, calculated from amino acid sequence
homodimer
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2 * 45000, SDS-PAGE
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homodimer
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2 * 46776, calculated from amino acid sequence
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homodimer
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2 * 48700, SDS-PAGE
homodimer
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2 * 48700, SDS-PAGE
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homodimer
2 * 43000, SDS-PAGE
homodimer
2 * 45047, calculated from sequence
homodimer
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2 * 43000, SDS-PAGE
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homodimer
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2 * 45047, calculated from sequence
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homodimer
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2 * 55000, calculated from amino acid sequence
homodimer
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2 * 55000, His-tagged enzyme, SDS-PAGE
homodimer
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2 * 55000, calculated from amino acid sequence
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homodimer
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2 * 49000, SDS-PAGE
homodimer
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immunoblotting
homotetramer
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homotetramer
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4 * 45000, SDS-PAGE
homotetramer
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actually a dimer of dimers
homotetramer
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4 * 55000, SDS-PAGE
homotetramer
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4 * 55000, SDS-PAGE
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homotetramer
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actually a dimer of dimers
homotetramer
4 * 52020, cytosolic isoform, sequence calculation, 4 * 53000, recombinant cytosolic isoform, SDS-PAGE
homotetramer
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4 * 52000, SDS-PAGE
homotetramer
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4 * 56000, SDS-PAGE
homotetramer
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4 * 53000, SDS-PAGE
homotetramer
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actually a dimer of dimers
homotetramer
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4 * 53000, SDS-PAGE
homotetramer
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actually a dimer of dimers
homotetramer
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4 * 53000, mutant enzyme
homotetramer
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actually a dimer of dimers
homotetramer
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lithium(dodecyl sulfate)-PAGE
homotetramer
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4 * 54000, SDS-PAGE
homotetramer
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4 * 56300, cytosol, SDS-PAGE
homotetramer
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4 * 53700, mitochondria, SDS-PAGE
homotetramer
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4 * 56300, cytosol, SDS-PAGE
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homotetramer
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4 * 53700, mitochondria, SDS-PAGE
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homotetramer
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actually a dimer of dimers
homotetramer
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4 * 53000, SDS-PAGE
homotetramer
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4 * 50000, SDS-PAGE
tetramer
4 * 50000, gel filtration
tetramer
x * 53000, SDS-PAGE, x * 53317, sequence analysis
tetramer
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x * 53000, SDS-PAGE, x * 53317, sequence analysis
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tetramer
isoform SHMT1, X-ray crystallography
tetramer
4 * 54000, SDS-PAGE, gel filtration
tetramer
4 * 54000 Da, gel filtration
tetramer
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4 * 54000, SDS-PAGE, gel filtration
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tetramer
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4 * 54000 Da, gel filtration
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tetramer
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4 * 53000, SDS-PAGE
tetramer
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4 * 53000, wild-type enzyme and mutant enzymes C203F and W110F, SDS-PAGE
tetramer
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4 * 50000, Western blot analysis
additional information
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the folding mechanism of SHMT is divided in two phases and terminates with pyridoxal 5'-phosphate binding. In the first one, the large and small domains rapidly assume their native state, forming a folding intermediate that is not able to bind pyridoxal 5'-phosphate. In the second, slower phase, the enzyme folds into the native structure, acquiring the capability to bind the cofactor. Importance of the third hydrophobic cluster, highly conserved in typr I fold enzymes, as key structural determinant of the assembly of eSHMT active site and overall native fold. This cluster plays a fundamental role in the transition from the first to the second phase of SHMT folding process
additional information
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the folding mechanism of SHMT is divided in two phases and terminates with pyridoxal 5'-phosphate binding. In the first one, the large and small domains rapidly assume their native state, forming a folding intermediate that is not able to bind pyridoxal 5'-phosphate. In the second, slower phase, the enzyme folds into the native structure, acquiring the capability to bind the cofactor. Importance of the third hydrophobic cluster, highly conserved in type I fold enzyme, as key structural determinant of the assembly of eSHMT active site and overall native fold. This cluster plays a fundamental role in the transition from the first to the second phase of SHMT folding process
additional information
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90% dimer and 10% tetramer in the same organism, one subunit: 45000 Da, SDS-PAGE