1JEF

TURKEY LYSOZYME COMPLEX WITH (GLCNAC)3

1JEF の概要

• エントリーDOI: 10.2210/pdb1jef/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900017
• 分子名称: LYSOZYME, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: enzyme, hydrolase, inhibitor complex, glycosidase, bacteriolytic enzyme
• 由来する生物種: Meleagris gallopavo (turkey)
• 細胞内の位置: Secreted: P00703
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14951.76

構造登録者

Harata, K.,Muraki, M. (登録日: 1997-04-23, 公開日: 1997-10-15, 最終更新日: 2024-10-16)

主引用文献

Harata, K.,Muraki, M.
X-ray structure of turkey-egg lysozyme complex with tri-N-acetylchitotriose. Lack of binding ability at subsite A.
Acta Crystallogr.,Sect.D, 53:650-657, 1997

PubMed Abstract: The turkey-egg lysozyme (TEL) complex with tri-N-acetylchitotriose [(GlcNac)3] was co-crystallized from 1.5% TEL and 2 mM (GlcNac)3 at pH 4.2. The crystal structure was determined by molecular replacement and refined to an R value of 0.182 using 10-1.77 A data. The (GlcNac)3 molecule occupies the subsites A, B and C. At the subsites B and C, the sugar residues are bound in a similar manner to that found in the hen-egg lysozyme (HEL) complex. In contrast, the GlcNac residue at the subsite A is exposed to bulk solvent and has no contact with the protein molecule because the active residue Asp101 in HEL is replaced by Gly in TEL. A sulfate ion is bound in the vicinity of subsite B and forms hydrogen bonds with the sugar residue and the guanidino group of Arg61, assisting the binding of the sugar residue to subsite B. The active-site cleft of TEL is narrower than that of native TEL, thus attaining the best fit of the (GlcNac)3 molecule. The lack of binding ability of subsite A is discussed in relation to the catalytic properties of TEL. The result suggests that the cleavage pattern of oligosaccharide substrates in the catalytic reaction is regulated by the protein-sugar interaction at subsite A.

PubMed: 15299852
DOI: 10.1107/S0907444997005362

実験手法

X-RAY DIFFRACTION (1.77 Å)