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Structure of IDP90567

Dihydroneopterin aldolase/dihydroneopterin triphosphate 2'-epimerase from Yersinia pestis.

Edit deposit information
CSGID target
IDP90567 
PDB Id
3R2E (NCBI MMDB
Authors
J.Osipiuk,N.Maltseva,M.Makowska-Grzyska,L.Papazisi,W.F.Anderson,A.Joachimiak,Center For Structural Genomics Of Infectious Diseases (Csgid) 
Responsible person
Jerzy Osipiuk 
Responsible lab
Argonne National Laboratory 
Deposition Date
Mar 14, 2011 
Release Date
Mar 23, 2011 

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 

Ligands

Ligand code Name Ligand type

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)  
Rall(%)
21.7 
Rwork(%)
21.5 (29.8) 
Rfree(%)
25.5 (29.8) 
Num. observed reflections
7960 (567) 
Num. Rfree reflections
366 (27) 
Completeness(%)
99.2 (98.6) 

Model parameters

Num Atoms
939  
Num Waters
11  
Num Hetatoms
0  
Model mean isotropic B factor
67.920Å2  
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