1TRG | Methyltransferase | date | May 21, 1998 ![]() |
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title | E. Coli Thymidylate Synthase In Symmetric Complex With Cb3717 And 2'-Deoxyuridine 5'-Monophosphate (Dump) | ||||||||||||||
authors | T.J.Stout, C.R.Sage, R.M.Stroud | ||||||||||||||
compound | source | ||||||||||||||
Molecule: Thymidylate Synthase Chain: Null Ec: 2.1.1.45 Engineered: Yes Biological_unit: Obligate Dimer |
Organism_scientific: Escherichia Coli Cell_line: X2913 Plasmid: Pthya-Wt Gene: Thya Expression_system: Escherichia Coli Expression_system_vector: Bluescript Vector Expression_system_plasmid: Pthya-Wt Expression_system_gene: Thya | ||||||||||||||
symmetry | Space Group: P 31 2 1 | R_factor | 0.180 | ||||||||||||
crystal cell |
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method | X-Ray Diffraction | resolution | 1.9 Å | ||||||||||||
ligand | CB3, CBX, UMP | enzyme | Thymidylate synthase;. DTMP synthase;. Thymidylate synthetase;. Methylenetetrahydrofolate. DUMP C-methyltransferase;. TMP synthetase. Transferase E.C.2.1.1.45 BRENDA | ||||||||||||
similarity | Belongs to the thymidylate synthase family.[Thymidylat_synt] | ||||||||||||||
subunit | Homodimer. | ||||||||||||||
catalytic activ. | 5,10-methylenetetrahydrofolate + dump = dihydrofolate + dtmp. | ||||||||||||||
pathway | Nucleotide biosynthesis; deoxyribonucleotide biosynthesis. | ||||||||||||||
post-translat. modifications | The n-terminus is carboxylated. | ||||||||||||||
subcellular loc. | Cytoplasm. | ||||||||||||||
genes | thyA (B. subtilis); TD, frd (B. T4); DFR1 (C. albicans); DHFR (G. gallus); TMP1 (C. neoformans); folA, thyA (E. coli); folA (H. volcanii); DHFR, TYMS (H. sapiens); folA, thyA (L. casei); Dhfr (M. musculus); THYA (P. carinii); Tyms (R. norvegicus); folA (T. maritima) | ||||||||||||||
function | This protein also binds to its mrna thus repressing its own translation. Provides the sole de novo source of dtmp for dna biosynthesis. | ||||||||||||||
Gene Ontology |
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disease | Anemia,megaloblastic,due to DHFR deficiency Thymidylate Synthetase; Tyms | ||||||||||||||
Primary reference | The additivity of substrate fragments in enzyme-ligand binding., Stout TJ, Sage CR, Stroud RM, Structure 1998 Jul 15;6(7):839-48. PMID:9687366 |
Data retrieval |
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Structure-derived information |
- Domain d1trg__, region [Jmol] [rasmolscript] [script source] |
Sequence-derived information |
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