Structural highlights
Function
FOSA_SERMA Metalloglutathione transferase which confers resistance to fosfomycin by catalyzing the addition of glutathione to fosfomycin.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structure of fosfomycin resistance protein FosA from transposon Tn2921.,Pakhomova S, Rife CL, Armstrong RN, Newcomer ME Protein Sci. 2004 May;13(5):1260-5. Epub 2004 Apr 9. PMID:15075406[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bernat BA, Laughlin LT, Armstrong RN. Fosfomycin resistance protein (FosA) is a manganese metalloglutathione transferase related to glyoxalase I and the extradiol dioxygenases. Biochemistry. 1997 Mar 18;36(11):3050-5. PMID:9115979 doi:http://dx.doi.org/10.1021/bi963172a
- ↑ Pakhomova S, Rife CL, Armstrong RN, Newcomer ME. Structure of fosfomycin resistance protein FosA from transposon Tn2921. Protein Sci. 2004 May;13(5):1260-5. Epub 2004 Apr 9. PMID:15075406 doi:10.1110/ps.03585004
