1BB7

LYSOZYME COMPLEX WITH 4-METHYL-UMBELLIFERYL CHITOBIOSE

1BB7 の概要

• エントリーDOI: 10.2210/pdb1bb7/pdb
• 分子名称: LYSOZYME, 4-METHYL-UMBELLIFERYL-N-ACETYL-CHITOBIOSE (3 entities in total)
• 機能のキーワード: hydrolase, n-acetyl-muramidase, umbelliferone glycosides
• 由来する生物種: Oncorhynchus mykiss (rainbow trout)
• 細胞内の位置: Secreted: P11941
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14885.62

構造登録者

Vollan, V.B.,Hough, E.,Karlsen, S. (登録日: 1998-04-29, 公開日: 1999-05-04, 最終更新日: 2024-11-20)

主引用文献

Vollan, V.B.,Hough, E.,Karlsen, S.
Structural studies on the binding of 4-methylumbelliferone glycosides of chitin to rainbow trout lysozyme.
Acta Crystallogr.,Sect.D, 55:60-66, 1999

PubMed Abstract: Two complexes between rainbow trout lysozyme (RBTL) and 4-methylumbelliferyl chitobioside, 4MeU-(GlcNAc)2, and chitotrioside, 4MeU-(GlcNAc)3, were produced by co-crystallization and soaking, respectively, and the crystal structures were solved at 2.0 A resolution. The results show that 4-MeU-(GlcNAc)3 binds in subsites A-D and that 4-MeU-(GlcNAc)2 binds in subsites B-D in the active-site cleft of RBTL. This agrees well with earlier crystallographic studies on the binding of oligosaccharides of chitin to RBTL, which showed that (GlcNAc)3 binds to sites B-D in RBTL and not to A-C as seen in the human and turkey egg-white lysozymes. For both complexes the 4-MeU moiety in site D has diffuse electron density and is flexible, as it is only bound to water molecules and not to the protein. Since no electron density was observed in site E, the solved structures give views of nonproductive enzyme-substrate complexes.

PubMed: 10089395
DOI: 10.1107/S0907444998006623

実験手法

X-RAY DIFFRACTION (2 Å)