Annotation

Description

D-ribulose-phosphate 3-epimerase from Francisella tularensis catalyses the conversion of D-ribulose 5-phosphate into D-xylulose 5-phosphate and is a part of the pentose phosphate pathway. This metabolic pathway is present in many bacteria and plants, but not animals, making proteins of this pathway a good target for the drug design. Subunits fold in a TIM barrel structure (beta/alpha 8-barrel). A sequence comparison with homologous epimerases outlined the active center and indicated that all members of this family are likely to share the same catalytic mechanism. The substrate could be modeled by putting its phosphate onto the observed sulfate position (between strands beta-7 and beta-8) and its epimerized C3 atom between two carboxylates that participate in an extensive hydrogen bonding system.  

Functional assignment

D-ribulose-phosphate 3-epimerase 

Structure information

Unit cell parameters

Space Group

F 41 3 2  

Unit Cell

a=224.08Å, b=224.08Å, c=224.08Å
α=90.00, β=90.00, γ=90.00 

Solvent content

71.86  

Matthews coefficient

4.37  

Refinement

Data for the highest resolution shell is in parentheses.

Resolution range

29.94-2.05Å (2.10-2.05Å)  

R_all(%)

15.9 

R_work(%)

15.8 (16.1) 

R_free(%)

17.7 (19.3) 

Num. observed reflections

30664 (2221) 

Num. R_free reflections

1533 (111) 

Completeness(%)

100.0 (100.0) 

Model parameters

Num Atoms

1728  

Num Waters

165  

Num Hetatoms

185  

Model mean isotropic B factor

13.420Ų  

RMSD bond length

0.012Å  

RMSD bond angle

1.396°  

Filename uploaded

rcsb054638.pdb (uploaded on Aug 18, 2009 2:27 PM)  

Inserted

Aug 18, 2009