1NPB

Crystal structure of the fosfomycin resistance protein from transposon Tn2921

Summary for 1NPB

• Entry DOI: 10.2210/pdb1npb/pdb
• Descriptor: fosfomycin-resistance protein, SULFATE ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: manganese binding, potassium binding loop, transferase
• Biological source: Serratia marcescens
• Cellular location: Cytoplasm: Q56415
• Total number of polymer chains: 6
• Total formula weight: 97454.35

Authors

Pakhomova, S.,Rife, C.L.,Armstrong, R.N.,Newcomer, M.E. (deposition date: 2003-01-17, release date: 2004-03-02, Last modification date: 2023-08-16)

Primary citation

Pakhomova, S.,Rife, C.L.,Armstrong, R.N.,Newcomer, M.E.
Structure of fosfomycin resistance protein FosA from transposon Tn2921.
Protein Sci., 13:1260-1265, 2004

PubMed Abstract: 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.

PubMed: 15075406
DOI: 10.1110/ps.03585004

Experimental method

X-RAY DIFFRACTION (2.5 Å)