Annotation

Description

This enzyme catalyses the deamination of asparagine to yield aspartic acid and an ammonium ion, resulting in a depletion of free circulatory asparagine in plasma. The enzyme from Yersinia pestis is type I L-asparageinase. The overall fold is similar to that of type II L-asparageinase of homotetrameric (dimer of intimate dimers) and the most of catalytic residues are conserved. However type I enzyme is just an intimate dimer, a half of that of type II L-asparageinase. The other key difference is the presence of the active-site flexible loop spanning a 14 – 28 beta-hairpin in the N-terminus including catalytic residues Thr14 and Tyr24. In type II enzyme, this loop serves as a mobile gate to the active site suggesting that in type I, this loop also serves as a gate but more restrictively. 

Functional assignment

 

Structure information

Unit cell parameters

Space Group

C 1 2 1  

Unit Cell

a=125.38Å, b=109.09Å, c=58.22Å
α=90.00, β=117.63, γ=90.00 

Solvent content

47.45  

Matthews coefficient

2.34  

Refinement

Data for the highest resolution shell is in parentheses.

Resolution range

38.92-1.90Å (1.97-1.90Å)  

R_all(%)

15.6 

R_work(%)

15.4 (21.1) 

R_free(%)

19.2 (23.8) 

Num. observed reflections

56883 (5146) 

Num. R_free reflections

2889 (249) 

Completeness(%)

99.2 (95.0) 

Model parameters

Num Atoms

5968  

Num Waters

503  

Num Hetatoms

0  

Model mean isotropic B factor

37.900Ų  

RMSD bond length

0.014Å  

RMSD bond angle

1.245°  

RMSD dihedral angle

15.274°

 

Filename uploaded

dep1w.pdb (uploaded on Jul 05, 2010 9:06 PM)  

Inserted

Jul 05, 2010