Annotation

Description

Folates are essential cofactors for various metabolic reactions involving one-carbon units. Mammals obtain folates from their diet, whereas most microorganisms synthesize folates de novo. Therefore, the folate biosynthetic pathway is a potential target for antimicrobial agents. Dihydroneopterin aldolase/dihydroneopterin triphosphate 2'-epimerase, a bifunctional protein, participates in folate biosynthesis. Dihydroneopterin aldolase (DHNA) catalyzes the conversion of 7,8-dihydroneopterin (DHNP) to 6-hydroxymethyl-7,8-dihydropterin (HP) with the generation of glycoaldehyde (GA). The second protein biological activity is the epimerization of carbon 2' of 7,8-dihydroneopterin (DHNP) and 7,8-dihydromonapterin (DHMP). 

Functional assignment

Lyase 

Structure information

Unit cell parameters

Space Group

I 4 2 2  

Unit Cell

a=71.72Å, b=71.72Å, c=107.63Å
α=90.00, β=90.00, γ=90.00 

Solvent content

 

Matthews coefficient

 

Refinement

Data for the highest resolution shell is in parentheses.

Resolution range

31.00-2.15Å (2.20-2.15Å)  

R_all(%)

21.7 

R_work(%)

21.5 (29.8) 

R_free(%)

25.5 (29.8) 

Num. observed reflections

7960 (567) 

Num. R_free reflections

366 (27) 

Completeness(%)

99.2 (98.6) 

Model parameters

Num Atoms

939  

Num Waters

11  

Num Hetatoms

0  

Model mean isotropic B factor

67.920Ų  

RMSD bond length

0.018Å  

RMSD bond angle

1.698°  

Filename uploaded

idp90567.pdb (uploaded on Mar 14, 2011 12:11 PM)  

Inserted

Mar 14, 2011