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Three‐dimesional structure of GlcNAcα1‐4Gal releasing Endo‐β‐Galactosidase from Clostridium perfringens
Author(s) -
Tempel Wolfram,
Liu ZhiJie,
Horanyi Peter S.,
Deng Lu,
Lee Doowon,
Newton M. Gary,
Rose John P.,
Ashida Hisashi,
Li SuChen,
Li YuTeh,
Wang BiCheng
Publication year - 2005
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.20363
Subject(s) - clostridium perfringens , chemistry , computational biology , microbiology and biotechnology , biology , bacteria , genetics
Introduction. Clostridium perfringens is a ubiquitous anaerobic bacterium that is commonly found not only in soil but also in the gastrointestinal tract of higher animals. Its pathogenicity has been reviewed extensively. As a major cause of gastrointestinal infections in humans and animals, C. perfringens is suspected to employ hydrolytic enzymes in the degradation of gastrointestinal mucous glycoproteins. A unique endo-galactosidase, Endo-GalGnGa, capable of releasing GlcNAc 1-4Gal from porcine gastric mucin was discovered serendipitously as a contaminant of a commercially available C. perfringens sialidase preparation. Further characterization revealed small but significant sequence similarities with known glycosidases, including several enzymes from Bacillus sp. Endo-GalGnGa has been cloned and overexpressed in Escherichia coli. Single-crystal X-ray diffraction studies of Endo-GalGnGa were undertaken in order to explain the distinctive behavior of these enzymes based on a structural model in atomic detail.