1XIX

Crystal Structure of Weissella viridescens FemX Form II

1XIX の概要

• エントリーDOI: 10.2210/pdb1xix/pdb
• 関連するPDBエントリー: 1LRZ 1NE9 1P4N 1XE4 1XF8
• 分子名称: FemX (2 entities in total)
• 機能のキーワード: crystal form ii, femx, ligase, transferase
• 由来する生物種: Weissella viridescens
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 38195.80

構造登録者

Biarrotte-Sorin, S.,Maillard, A.P.,Arthur, M.,Mayer, C. (登録日: 2004-09-22, 公開日: 2005-05-31, 最終更新日: 2023-08-23)

主引用文献

Maillard, A.P.,Biarrotte-Sorin, S.,Villet, R.,Mesnage, S.,Bouhss, A.,Sougakoff, W.,Mayer, C.,Arthur, M.
Structure-Based Site-Directed Mutagenesis of the UDP-MurNAc-Pentapeptide-Binding Cavity of the FemX Alanyl Transferase from Weissella viridescens
J.Bacteriol., 187:3833-3838, 2005

PubMed Abstract: Weissella viridescens FemX (FemX(Wv)) belongs to the Fem family of nonribosomal peptidyl transferases that use aminoacyl-tRNA as the amino acid donor to synthesize the peptide cross-bridge found in the peptidoglycan of many species of pathogenic gram-positive bacteria. We have recently solved the crystal structure of FemX(Wv) in complex with the peptidoglycan precursor UDP-MurNAc-pentapeptide and report here the site-directed mutagenesis of nine residues located in the binding cavity for this substrate. Two substitutions, Lys36Met and Arg211Met, depressed FemX(Wv) transferase activity below detectable levels without affecting protein folding. Analogues of UDP-MurNAc-pentapeptide lacking the phosphate groups or the C-terminal D-alanyl residues were not substrates of the enzyme. These results indicate that Lys36 and Arg211 participate in a complex hydrogen bond network that connects the C-terminal D-Ala residues to the phosphate groups of UDP-MurNAc-pentapeptide and constrains the substrate in a conformation that is essential for transferase activity.

PubMed: 15901708
DOI: 10.1128/JB.187.11.3833-3838.2005

実験手法

X-RAY DIFFRACTION (2 Å)