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Structure of IDP04293

Structure of phosphotransferase enzyme II, A component from Yersinia pestis CO92 at 1.2 A resolution

Edit deposit information
CSGID target
IDP04293 
PDB Id
3OXP (NCBI MMDB
Authors
E.V.Filippova,Z.Wawrzak,M.Kudritska,A.Edwards,A.Savchenko,W.F.Anderson,Center For Structural Genomics Of Infectious Diseases (Csgid) 
Responsible person
Ekaterina Filippova 
Responsible lab
Northwestern University 
Deposition Date
Sep 21, 2010 
Release Date
Oct 13, 2010 

Annotation

Description
The bacterial phosphoenolpyruvate-dependent sugar phosphotransferase system (PEP-PTS) is essential in the coupled transportation and phosphorylation of various types of carbohydrates. The PtxA protein from Yersinia pestis CO92 are sequentially similar to the mannitol-specific cryptic phosphotransferase MtlA. The PtxA protein corresponds to the phosphotransferase enzyme IIA component.The structure of PtxA adopts a globular fold consisting of a central mixed five-strand beta-sheet flanked by seven helices at both sides. Here we report the solution structure at high resolution by X-ray crystallography.  
Functional assignment
Amino acid biosynthesis 

Ligands

Ligand code Name Ligand type
GOL crystallization
MSE modified residue
175 3,5-dihydro-5-methylidene-4h-imidazol-4-on

Structure information

Unit cell parameters

Space Group
P 21 21 21  
Unit Cell

a=56.91Å, b=57.95Å, c=78.74Å
α=90.00, β=90.00, γ=90.00 
Solvent content
38.52  
Matthews coefficient
2  

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
46.67-1.20Å (1.23-1.20Å)  
Rall(%)
14.8 
Rwork(%)
14.7 (23.2) 
Rfree(%)
17.9 (26.9) 
Num. observed reflections
81630 (5899) 
Num. Rfree reflections
4081 (262) 
Completeness(%)
99.6 (98.3) 

Model parameters

Num Atoms
2739  
Num Waters
410  
Num Hetatoms
0  
Model mean isotropic B factor
10.720Å2  
RMSD bond length
0.018Å  
RMSD bond angle
1.718°  
Filename uploaded
cycle_best_1_refmac18.pdb (uploaded on Sep 21, 2010 4:55 PM)  
Inserted
Sep 21, 2010