Structure of IDP00060
CrCrystal Structure of Metallothiol Transferase FosB 2 from Bacillus anthracis str. Ames
Edit deposit information
- CSGID target
- IDP00060
- PDB Id
- 4JD1 (NCBI MMDB)
- Authors
- N.Maltseva,Y.Kim,R.Jedrzejczak,S.V.Sharma,C.J.Hamilton,W.F.Anderson,A.Joachimiak,Center For Structural Genomics Of Infectious Diseases (Csgid)
- Responsible person
- Natalia Maltseva
- Responsible lab
- Argonne National Laboratory
- Deposition Date
- Feb 22, 2013
- Release Date
- Mar 20, 2013
Annotation
- Description
- FosB along with FosA , and FosX are so far indentified types of thiol transferase enzymes with slightly different mechanism that confer resistance to fosfomycin. Fosfomycin [(1R,2S)-epoxypropylphosphonic acid] is a clinically important, broad-spectrum antibiotic that irreversibly inactivates MurA, which catalyzes the first committed step in peptidoglycan biosynthesis. Crystal structure of metallothiol transferase FosB 2 from Bacillus anthracis complexed with fosfomycin was solved at 1.7A. The protein has alpha-beta fold and forms homodimer. Overall the structure is very similar to that of FosA including the metal binding site.
- Functional assignment
Ligands
| Ligand code | Name | Ligand type |
|---|---|---|
| 175 | 3,5-dihydro-5-methylidene-4h-imidazol-4-on | biological |
| FCN | fosfomycin | crystallization |
| PGE | crystallization |
Structure information
Unit cell parameters
- Space Group
- P 43
- Unit Cell
-
a=48.16Å, b=48.16Å, c=147.59Å
α=90.00, β=90.00, γ=90.00 - Solvent content
- Matthews coefficient
- Resolution range
- 34.41-1.70Å (1.75-1.70Å)
- Rall(%)
- 17.4
- Rwork(%)
- 17.2 (26.0)
- Rfree(%)
- 19.3 (23.0)
- Num. observed reflections
- 38394 (2796)
- Num. Rfree reflections
- 1919 (133)
- Completeness(%)
- 99.4 (94.0)
- Num Atoms
- 2560
- Num Waters
- 184
- Num Hetatoms
- 202
- Model mean isotropic B factor
- 30.650Å2
- RMSD bond length
- 0.011Å
- RMSD bond angle
- 1.450°
- RMSD dihedral angle
- 19.5°
- Filename uploaded
- dep.pdb (uploaded on Apr 18, 2013 11:56 AM)
- Inserted
- Apr 18, 2013