1eg7 Citations

The crystal structure of N(10)-formyltetrahydrofolate synthetase from Moorella thermoacetica.

Biochemistry 39 3920-6 (2000)
Cited: 18 times
EuropePMC logo PMID: 10747779

Abstract

The structure was solved at 2.5 A resolution using multiwavelength anomalous dispersion (MAD) scattering by Se-Met residues. The subunit of N(10)-formyltetrahydrofolate synthetase is composed of three domains organized around three mixed beta-sheets. There are two cavities between adjacent domains. One of them was identified as the nucleotide binding site by homology modeling. The large domain contains a seven-stranded beta-sheet surrounded by helices on both sides. The second domain contains a five-stranded beta-sheet with two alpha-helices packed on one side while the other two are a wall of the active site cavity. The third domain contains a four-stranded beta-sheet forming a half-barrel. The concave side is covered by two helices while the convex side is another wall of the large cavity. Arg 97 is likely involved in formyl phosphate binding. The tetrameric molecule is relatively flat with the shape of the letter X, and the active sites are located at the end of the subunits far from the subunit interface.

Articles - 1eg7 mentioned but not cited (1)

  1. Mechanism of N10-formyltetrahydrofolate synthetase derived from complexes with intermediates and inhibitors. Celeste LR, Chai G, Bielak M, Minor W, Lovelace LL, Lebioda L. Protein Sci 21 219-228 (2012)


Reviews citing this publication (5)

  1. Acetogenesis and the Wood-Ljungdahl pathway of CO(2) fixation. Ragsdale SW, Pierce E. Biochim Biophys Acta 1784 1873-1898 (2008)
  2. Old acetogens, new light. Drake HL, Gössner AS, Daniel SL. Ann N Y Acad Sci 1125 100-128 (2008)
  3. Physiology of the thermophilic acetogen Moorella thermoacetica. Drake HL, Daniel SL. Res Microbiol 155 869-883 (2004)
  4. Advances in multiple wavelength anomalous diffraction crystallography. Ealick SE. Curr Opin Chem Biol 4 495-499 (2000)
  5. Physiology of the thermophilic acetogen Moorella thermoacetica. Drake HL, Daniel SL. Res Microbiol 155 422-436 (2004)

Articles citing this publication (12)

  1. Classification and evolution of P-loop GTPases and related ATPases. Leipe DD, Wolf YI, Koonin EV, Aravind L. J Mol Biol 317 41-72 (2002)
  2. The MTHFD1 p.Arg653Gln variant alters enzyme function and increases risk for congenital heart defects. Christensen KE, Rohlicek CV, Andelfinger GU, Michaud J, Bigras JL, Richter A, Mackenzie RE, Rozen R. Hum Mutat 30 212-220 (2009)
  3. Recovery and analysis of formyltetrahydrofolate synthetase gene sequences from natural populations of acetogenic bacteria. Leaphart AB, Lovell CR. Appl Environ Microbiol 67 1392-1395 (2001)
  4. Biochemical fossils of the ancient transition from geoenergetics to bioenergetics in prokaryotic one carbon compound metabolism. Sousa FL, Martin WF. Biochim Biophys Acta 1837 964-981 (2014)
  5. Real-time PCR assays targeting formyltetrahydrofolate synthetase gene to enumerate acetogens in natural and engineered environments. Xu K, Liu H, Du G, Chen J. Anaerobe 15 204-213 (2009)
  6. Presence of novel, potentially homoacetogenic bacteria in the rumen as determined by analysis of formyltetrahydrofolate synthetase sequences from ruminants. Henderson G, Naylor GE, Leahy SC, Janssen PH. Appl Environ Microbiol 76 2058-2066 (2010)
  7. Purification of the formate-tetrahydrofolate ligase from Methylobacterium extorquens AM1 and demonstration of its requirement for methylotrophic growth. Marx CJ, Laukel M, Vorholt JA, Lidstrom ME. J Bacteriol 185 7169-7175 (2003)
  8. A novel mouse model for genetic variation in 10-formyltetrahydrofolate synthetase exhibits disturbed purine synthesis with impacts on pregnancy and embryonic development. Christensen KE, Deng L, Leung KY, Arning E, Bottiglieri T, Malysheva OV, Caudill MA, Krupenko NI, Greene ND, Jerome-Majewska L, MacKenzie RE, Rozen R. Hum Mol Genet 22 3705-3719 (2013)
  9. Formyltetrahydrofolate synthetase sequences from salt marsh plant roots reveal a diversity of acetogenic bacteria and other bacterial functional groups. Leaphart AB, Friez MJ, Lovell CR. Appl Environ Microbiol 69 693-696 (2003)
  10. Site-directed mutagenesis of a potential catalytic and formyl phosphate binding site and substrate inhibition of N10-formyltetrahydrofolate synthetase. Leaphart AB, Trent Spencer H, Lovell CR. Arch Biochem Biophys 408 137-143 (2002)
  11. The enzymes of the 10-formyl-tetrahydrofolate synthetic pathway are found exclusively in the cytosol of the trypanosomatid parasite Leishmania major. Vickers TJ, Murta SM, Mandell MA, Beverley SM. Mol Biochem Parasitol 166 142-152 (2009)
  12. Letter Time passes yet errors remain: comments on the structure of N10-formyltetrahydrofolate synthetase. Stec B. Protein Sci 22 671-674 (2013)