2SLI

LEECH INTRAMOLECULAR TRANS-SIALIDASE COMPLEXED WITH 2,7-ANHYDRO-NEU5AC, THE REACTION PRODUCT

2SLI の概要

• エントリーDOI: 10.2210/pdb2sli/pdb
• 分子名称: INTRAMOLECULAR TRANS-SIALIDASE, 2-ACETYLAMINO-7-(1,2-DIHYDROXY-ETHYL)-3-HYDROXY-6,8-DIOXA-BICYCLO[3.2.1]OCTANE-5-CARBOXYLIC ACID (3 entities in total)
• 機能のキーワード: hydrolase, intramolecular trans-sialidase, neuraminidase
• 由来する生物種: Macrobdella decora (North American leech)
• 細胞内の位置: Secreted, extracellular space: Q27701
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 74856.94

構造登録者

Luo, Y.,Li, S.C.,Li, Y.T.,Luo, M. (登録日: 1998-10-03, 公開日: 1999-04-27, 最終更新日: 2024-04-03)

主引用文献

Luo, Y.,Li, S.C.,Li, Y.T.,Luo, M.
The 1.8 A structures of leech intramolecular trans-sialidase complexes: evidence of its enzymatic mechanism.
J.Mol.Biol., 285:323-332, 1999

PubMed Abstract: Intramolecular trans-sialidase from leech (Macrobdella decora) is the first member of the sialidase superfamily found to exhibit strict specificity towards the cleavage of terminal Neu5Acalpha2-->3Gal linkage in sialoglycoconjugates. Its release of 2,7-anhydro-Neu5Ac instead of Neu5Ac indicates that it catalyzes an intramolecular trans-sialosyl reaction. Crystal structures of its complexes with an inactive substrate analogue 2-propenyl-Neu5Ac, and with the product 2,7-anhydro-Neu5Ac, have been determined to 1.8 A resolution. The boat conformation of the pyranose observed in the complexes supports the proposed enzymatic mechanism that O7 of an axial 6-glycerol group attacks the positively charged C2 of the intermediate. A generalized mechanism is proposed for the sialidase superfamily.

PubMed: 9878409
DOI: 10.1006/jmbi.1998.2345

実験手法

X-RAY DIFFRACTION (1.8 Å)