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Structure of IDP00427

The crystal structure of the bifunctional N- acetylglucosamine-1-phosphate Uridyltransferase/Glucosamine-1-Phosphate acetyltransferase from Yersinia pestis CO92

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CSGID target
IDP00427 
PDB Id
3FWW (NCBI MMDB) 
Authors
R.Zhang,M.Gu,J.Stam,W.Anderson,A.Joachimiak,Center For Structural Genomics Of Infectious Diseases (Csgid) 
Responsible person
Rong-guang Zhang 
Responsible lab
Argonne National Laboratory 
Deposition Date
Jan 19, 2009 
Release Date
Mar 24, 2009 

Annotation

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Description
N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU) from Yersinia pestis is a bifunctional enzyme that catalyzes both the acetyltransfer and uridyltransfer reactions in the prokaryotic UDP-GlcNAc biosynthetic pathway. This 2.5A structure from Yersinia pestis is very similar to the other GlmU structures solved from different organisms. With one molecule per asymmetric unit, the monomers from three neighbouring asymmetric units related by the crystal threefold formed a biological trimer. 
Functional assignment
N-acetylglucosamine-1-phosphate uridyltransferase (GlmU)  

Ligands

Ligand code Name Ligand type

Structure information

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Unit cell parameters

Space Group
P 63 2 2  
Unit Cell

a=88.32Å, b=88.32Å, c=251.93Å
α=90.00, β=90.00, γ=120.00 
Solvent content
57.59  
Matthews coefficient
2.9  

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
34.80-2.50Å (0.00-0.00Å)  
Rall(%)
21.7 
Rwork(%)
21.4 (0.0) 
Rfree(%)
27.7 (0.0) 
Num. observed reflections
21518 (0) 
Num. Rfree reflections
1103 (0) 
Completeness(%)
96.2 (0.0) 

Model parameters

Num Atoms
3330  
Num Waters
25  
Num Hetatoms
26  
Model mean isotropic B factor
79.612Å2  
RMSD bond length
0.000Å  
RMSD bond angle
0.000°  
Filename uploaded
rcsb051143.pdb (uploaded on Jan 22, 2009 11:28 AM)  
Inserted
Jan 22, 2009