1JA7

BINDING OF N-ACETYLGLUCOSAMINE TO CHICKEN EGG LYSOZYME: A POWDER DIFFRACTION STUDY

1JA7 の概要

• エントリーDOI: 10.2210/pdb1ja7/pdb
• 関連するPDBエントリー: 1JA2 1JA4 1JA6
• 分子名称: LYSOZYME, 2-acetamido-2-deoxy-alpha-D-glucopyranose (2 entities in total)
• 機能のキーワード: powder diffraction, rietveld refinement, lysozyme, hydrolase
• 由来する生物種: Gallus gallus (chicken)
• 細胞内の位置: Secreted: P00698
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14552.37

構造登録者

Von Dreele, R.B. (登録日: 2001-05-29, 公開日: 2001-06-15, 最終更新日: 2024-10-30)

主引用文献

Von Dreele, R.B.
Binding of N-acetylglucosamine to chicken egg lysozyme: a powder diffraction study.
Acta Crystallogr.,Sect.D, 57:1836-1842, 2001

PubMed Abstract: The binding of N-acetylglucosamine (NAG) to chicken egg lysozyme (E.C. 3.2.1.17) was investigated by high-resolution X-ray powder diffraction at room temperature. NAG was found to bind to lysozyme in a rapid precipitation preparation with 0.05 M NaCl buffer pH 6.0, but not 0.05 M NaCl buffer pH 5.0. Binding was indicated by significant and readily apparent changes in the diffraction pattern from that of the apo protein precipitated from the same solvent. The location of NAG bound to lysozyme was easily found from a difference Fourier map generated from structure factors extracted during a preliminary combined Rietveld and stereochemical restraint refinement. Full protein and protein-NAG structures were refined with these techniques (R(wp) = 2.22-2.49%, R(p) = 1.79-1.95%, R(F)(2) = 4.95-6.35%) and revealed a binding mode for NAG which differed from that found in an earlier single-crystal study and probably represents a precursor trapped by rapid precipitation.

PubMed: 11717496
DOI: 10.1107/S0907444901015748

実験手法

POWDER DIFFRACTION