1NPB

Crystal structure of the fosfomycin resistance protein from transposon Tn2921

1NPB の概要

• エントリーDOI: 10.2210/pdb1npb/pdb
• 分子名称: fosfomycin-resistance protein, SULFATE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: manganese binding, potassium binding loop, transferase
• 由来する生物種: Serratia marcescens
• 細胞内の位置: Cytoplasm: Q56415
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 97454.35

構造登録者

Pakhomova, S.,Rife, C.L.,Armstrong, R.N.,Newcomer, M.E. (登録日: 2003-01-17, 公開日: 2004-03-02, 最終更新日: 2023-08-16)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.5 Å)