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Structure of IDP01849

Methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase, putative bifunctional protein from Francisella tularensis.

Edit deposit information
CSGID target
IDP01849 
PDB Id
3L07 (NCBI MMDB
Authors
J.Osipiuk,N.Maltseva,R.Mulligan,J.Hasseman,W.F.Anderson,A.Joachimiak 
Responsible person
Jerzy Osipiuk 
Responsible lab
Argonne National Laboratory 
Deposition Date
Dec 09, 2009 
Release Date
Dec 22, 2009 

Annotation

Description
Methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase catalyzes the formation of 5,10-methenyl-tetrahydrofolate (5,10-methenyl-THF) from 5,10-methylene-THF and subsequent formation of 10-formyl-THF from 5,10-methenyltetrahydrofolate. 5,10-methylene-THF is a substrate for thymidylate synthetase, while 10-formyl-THF is a formyl group donor in purine and formylmethionine-tRNA syntheses. A variety of human pathologies, including conditions such as spina bifida and hyperhomocysteinemia, are related to metabolic or dietary folate deficiencies. 5,10-methylene-THF dehydrogenase and cyclohydrolase activities are generally found on a single, bifunctional enzyme in bacteria and in most mitochondria. The bacterial enzymes and cytosolic enzymes of eukaryotes are predominantly NADP dependent, whereas most mitochondrial enzymes and monofunctional dehydrogenases use NAD. These enzymes bind a single folate substrate and a single NADP coenzyme per subunit.  
Functional assignment
 

Ligands

Ligand code Name Ligand type
IMD
PO4 PHOSPHATE ION
EDO
ACT

Structure information

Unit cell parameters

Space Group
P 21 21 21  
Unit Cell

a=70.30Å, b=73.39Å, c=106.92Å
α=90.00, β=90.00, γ=90.00 
Solvent content
45.11  
Matthews coefficient
2.24  

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
43.30-1.88Å (1.93-1.88Å)  
Rall(%)
16.8 
Rwork(%)
16.5 (22.4) 
Rfree(%)
20.8 (28.0) 
Num. observed reflections
45643 (3183) 
Num. Rfree reflections
2282 (164) 
Completeness(%)
99.6 (96.2) 

Model parameters

Num Atoms
4908  
Num Waters
437  
Num Hetatoms
0  
Model mean isotropic B factor
15.090Å2  
RMSD bond length
0.020Å  
RMSD bond angle
1.663°  
Filename uploaded
idp01849.pdb (uploaded on Dec 09, 2009 3:25 PM)  
Inserted
Dec 09, 2009