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Structure of IDP01372

The crystal structure of the UDP-N-acetylenolpyruvoylglucosamine reductase from the Vibrio cholerae O1 biovar E1 Tor

Edit deposit information
CSGID target
IDP01372 
PDB Id
3I99 (NCBI MMDB
Authors
'R.Zhang,M.Gu,S.Peterson,W.Anderson,A.Joachimiak,Center For Structural Genomics Of Infectious Diseases (Csgid)' 
Responsible person
Rong-guang Zhang 
Responsible lab
Argonne National Laboratory 
Deposition Date
Jul 10, 2009 
Release Date
Oct 20, 2009 

Annotation

Description
The enzymes essential for bacterial peptidoglycan biosynthesis are attractive targets for antimicrobial drug development. One of these is MurB, which contains FAD as a cofactor and catalyzes the NADPH-dependent reduction of UDP-N-acetylenolpyruvylglucosamine (UDP-GlcNAcEP) to UDP-N-acetylmuramic acid. The X-ray crystal structure of the substrate FAD form of UDP-N-acetylenolpyruvylglucosamine reductase (MurB) from Vibrio cholerae O1 biovar EI Tor has been solved to 2.0 A resolution. As compared with MurB of Staphylococcus aureus, the overall structures are similar, but there are big difference in the loop regions (197-214,242-275) and also in the N and C terminals.  
Functional assignment
UDP-N-acetylenolpyruvylglucosamine 

Ligands

Ligand code Name Ligand type
FAD
PO4
MSE modified residue

Structure information

Unit cell parameters

Space Group
P 43  
Unit Cell

a=84.33Å, b=84.33Å, c=53.34Å
α=90.00, β=90.00, γ=90.00 
Solvent content
48.36  
Matthews coefficient
2.38  

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
59.66-2.20Å (2.26-2.20Å)  
Rall(%)
17.1 
Rwork(%)
16.8 (24.9) 
Rfree(%)
22.3 (30.0) 
Num. observed reflections
19123 (1369) 
Num. Rfree reflections
975 (57) 
Completeness(%)
99.3 (96.8) 

Model parameters

Num Atoms
2803  
Num Waters
114  
Num Hetatoms
0  
Model mean isotropic B factor
27.480Å2  
RMSD bond length
0.022Å  
RMSD bond angle
2.041°  
Filename uploaded
IDP1372_2pdb.pdb (uploaded on Aug 10, 2009 11:34 AM)  
Inserted
Aug 10, 2009