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PDBsum entry 1eg7

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protein ligands links
Ligase PDB id
1eg7
Jmol
Contents
Protein chains
549 a.a. *
Ligands
SO4 ×11
Waters ×269
* Residue conservation analysis
PDB id:
1eg7
Name: Ligase
Title: The crystal structure of formyltetrahydrofolate synthetase f moorella thermoacetica
Structure: Formyltetrahydrofolate synthetase. Chain: a, b. Engineered: yes
Source: Moorella thermoacetica. Organism_taxid: 1525. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PDB file)
Resolution:
2.50Å     R-factor:   0.253     R-free:   0.301
Authors: R.Radfar,R.Shin,G.M.Sheldrick,W.Minor,C.R.Lovell,J.D.Odom,R. L.Lebioda
Key ref:
R.Radfar et al. (2000). The crystal structure of N(10)-formyltetrahydrofolate synthetase from Moorella thermoacetica. Biochemistry, 39, 3920-3926. PubMed id: 10747779 DOI: 10.1021/bi992790z
Date:
14-Feb-00     Release date:   14-Feb-01    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P21164  (FTHS_MOOTH) -  Formate--tetrahydrofolate ligase
Seq:
Struc:
 
Seq:
Struc:
559 a.a.
549 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.6.3.4.3  - Formate--tetrahydrofolate ligase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Folate Coenzymes
      Reaction: ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate
ATP
+ formate
+ tetrahydrofolate
= ADP
+ phosphate
+ 10-formyltetrahydrofolate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     tetrahydrofolate interconversion   3 terms 
  Biochemical function     nucleotide binding     4 terms  

 

 
    reference    
 
 
DOI no: 10.1021/bi992790z Biochemistry 39:3920-3926 (2000)
PubMed id: 10747779  
 
 
The crystal structure of N(10)-formyltetrahydrofolate synthetase from Moorella thermoacetica.
R.Radfar, R.Shin, G.M.Sheldrick, W.Minor, C.R.Lovell, J.D.Odom, R.B.Dunlap, L.Lebioda.
 
  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.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20118378 G.Henderson, G.E.Naylor, S.C.Leahy, and P.H.Janssen (2010).
Presence of novel, potentially homoacetogenic bacteria in the rumen as determined by analysis of formyltetrahydrofolate synthetase sequences from ruminants.
  Appl Environ Microbiol, 76, 2058-2066.  
18767138 K.E.Christensen, C.V.Rohlicek, G.U.Andelfinger, J.Michaud, J.L.Bigras, A.Richter, R.E.Mackenzie, and R.Rozen (2009).
The MTHFD1 p.Arg653Gln variant alters enzyme function and increases risk for congenital heart defects.
  Hum Mutat, 30, 212-220.  
19450731 T.J.Vickers, S.M.Murta, M.A.Mandell, and S.M.Beverley (2009).
The enzymes of the 10-formyl-tetrahydrofolate synthetic pathway are found exclusively in the cytosol of the trypanosomatid parasite Leishmania major.
  Mol Biochem Parasitol, 166, 142-152.  
18378590 H.L.Drake, A.S.Gössner, and S.L.Daniel (2008).
Old acetogens, new light.
  Ann N Y Acad Sci, 1125, 100-128.  
18801467 S.W.Ragsdale, and E.Pierce (2008).
Acetogenesis and the Wood-Ljungdahl pathway of CO(2) fixation.
  Biochim Biophys Acta, 1784, 1873-1898.  
12514064 A.B.Leaphart, M.J.Friez, and C.R.Lovell (2003).
Formyltetrahydrofolate synthetase sequences from salt marsh plant roots reveal a diversity of acetogenic bacteria and other bacterial functional groups.
  Appl Environ Microbiol, 69, 693-696.  
14645277 C.J.Marx, M.Laukel, J.A.Vorholt, and M.E.Lidstrom (2003).
Purification of the formate-tetrahydrofolate ligase from Methylobacterium extorquens AM1 and demonstration of its requirement for methylotrophic growth.
  J Bacteriol, 185, 7169-7175.  
11229939 A.B.Leaphart, and C.R.Lovell (2001).
Recovery and analysis of formyltetrahydrofolate synthetase gene sequences from natural populations of acetogenic bacteria.
  Appl Environ Microbiol, 67, 1392-1395.  
11087401 R.Radfar, A.Leaphart, J.M.Brewer, W.Minor, J.D.Odom, R.B.Dunlap, C.R.Lovell, and L.Lebioda (2000).
Cation binding and thermostability of FTHFS monovalent cation binding sites and thermostability of N10-formyltetrahydrofolate synthetase from Moorella thermoacetica.
  Biochemistry, 39, 14481-14486.
PDB codes: 1fp7 1fpm
11006535 S.E.Ealick (2000).
Advances in multiple wavelength anomalous diffraction crystallography.
  Curr Opin Chem Biol, 4, 495-499.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.