Annotation

Description

D-Glutamic acid is a required biosynthetic building block for peptidoglycan, and the enzyme glutamate racemase (GluR) catalyzes the inter-conversion of D and L-glutamate enantiomers. Therefore, GluR is considered as an attractive target for the design of new antibacterial drugs. Here, we report the crystal structure of GluR from Francisella tularensis subsp. tularensis SCHU S4 in complex with D-glutamate, which provides a basis for designing narrow-spectrum antimicrobial agents.  

Functional assignment

Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan 

Structure information

Unit cell parameters

Space Group

P 43 21 2  

Unit Cell

a=98.06Å, b=98.06Å, c=154.15Å
α=90.00, β=90.00, γ=90.00 

Solvent content

40.37  

Matthews coefficient

2.06  

Refinement

Data for the highest resolution shell is in parentheses.

Resolution range

25.22-1.65Å (1.69-1.65Å)  

R_all(%)

16.4 

R_work(%)

16.3 (23.2) 

R_free(%)

19.3 (27.2) 

Num. observed reflections

90648 (6621) 

Num. R_free reflections

4532 (326) 

Completeness(%)

99.9 (99.7) 

Model parameters

Num Atoms

6194  

Num Waters

601  

Num Hetatoms

764  

Model mean isotropic B factor

12.400Ų  

RMSD bond length

0.017Å  

RMSD bond angle

1.537°  

Filename uploaded

rcsb061600.pdb (uploaded on Sep 17, 2010 12:54 PM)  

Inserted

Sep 17, 2010