PDBsum entry 1npb

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protein ligands Protein-protein interface(s) links
Transferase PDB id
Protein chains
(+ 0 more) 140 a.a. *
SO4 ×10
GOL ×7
Waters ×348
* Residue conservation analysis
PDB id:
Name: Transferase
Title: Crystal structure of the fosfomycin resistance protein from tn2921
Structure: Fosfomycin-resistance protein. Chain: a, b, c, d, e, f. Engineered: yes
Source: Serratia marcescens. Organism_taxid: 615. Gene: tn2921. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Biol. unit: Dimer (from PQS)
2.50Å     R-factor:   0.185     R-free:   0.230
Authors: S.Pakhomova,C.L.Rife,R.N.Armstrong,M.E.Newcomer
Key ref:
S.Pakhomova et al. (2004). Structure of fosfomycin resistance protein FosA from transposon Tn2921. Protein Sci, 13, 1260-1265. PubMed id: 15075406 DOI: 10.1110/ps.03585004
17-Jan-03     Release date:   02-Mar-04    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
Q56415  (FOSA_SERMA) -  Glutathione transferase FosA
141 a.a.
140 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Glutathione transferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: RX + glutathione = HX + R-S-glutathione
+ glutathione
= HX
+ R-S-glutathione
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     metabolic process   2 terms 
  Biochemical function     transferase activity     3 terms  


DOI no: 10.1110/ps.03585004 Protein Sci 13:1260-1265 (2004)
PubMed id: 15075406  
Structure of fosfomycin resistance protein FosA from transposon Tn2921.
S.Pakhomova, C.L.Rife, R.N.Armstrong, M.E.Newcomer.
The crystal structure of fosfomycin resistance protein FosA from transposon Tn2921 has been established at a resolution of 2.5 A. The protein crystallized without bound Mn(II) and K+, ions crucial for efficient catalysis, providing a structure of the apo enzyme. The protein maintains the three-dimensional domain-swapped arrangement of the paired betaalphabetabetabeta-motifs observed in the genomically encoded homologous enzyme from Pseudomonas aeruginosa (PA1129). The basic architecture of the active site is also maintained, despite the absence of the catalytically essential Mn(II). However, the absence of K+, which has been shown to enhance enzymatic activity, appears to contribute to conformational heterogeneity in the K(+)-binding loops.
  Selected figure(s)  
Figure 2.
Figure 2. View of the FosA dimer. (A) A stereo view of FosA dimer along a twofold NCS symmetry axis with bound sulfate ions and glycerol molecules. Monomers A and B are shown in green and yellow, respectively. (B) A stereo view of superposition of FosA (magenta) and PA1129 (blue) dimers. (C) A trimer of dimers as observed in the asymmetric unit of the FosA structure. Pictures 2-4 were made by using SETOR (Evans 1993).
Figure 4.
Figure 4. (A) The active site cavity of subunit A of FosA with bound sulfate ions. Superimposed active site residues, Mn(II), fosfomycin, and K+ loop from PA1129 FosA are shown in pink. (B) Close-up stereo view of the active site.
  The above figures are reprinted by permission from the Protein Society: Protein Sci (2004, 13, 1260-1265) copyright 2004.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21212150 V.N.De Groote, M.Fauvart, C.I.Kint, N.Verstraeten, A.Jans, P.Cornelis, and J.Michiels (2011).
Pseudomonas aeruginosa fosfomycin resistance mechanisms affect non-inherited fluoroquinolone tolerance.
  J Med Microbiol, 60, 329-336.  
19477421 H.Xu, Y.Zhang, J.Yang, T.Mahmud, L.Bai, and Z.Deng (2009).
Alternative epimerization in C(7)N-aminocyclitol biosynthesis is catalyzed by ValD, a large protein of the vicinal oxygen chelate superfamily.
  Chem Biol, 16, 567-576.  
19016852 N.Allocati, L.Federici, M.Masulli, and C.Di Ilio (2009).
Glutathione transferases in bacteria.
  FEBS J, 276, 58-75.  
19101977 X.Wu, P.M.Flatt, H.Xu, and T.Mahmud (2009).
Biosynthetic Gene Cluster of Cetoniacytone A, an Unusual Aminocyclitol from the Endosymbiotic Bacterium Actinomyces sp. Lu 9419.
  Chembiochem, 10, 304-314.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.