structural relationships in the lysozyme superfamily significant evidence for glycoside hydrolase signature motifs溶菌酶的结构关系总科重要的证据糖苷水解酶签名主题.pdfVIP

Structural Relationships in the Lysozyme Superfamily: Significant Evidence for Glycoside Hydrolase Signature Motifs ¨ 1 ¨ 2 2 ´ 2,3 Alexandre Wohlkonig , Joelle Huet , Yvan Looze , Rene Wintjens * ´ ´ ´ 1 Structural Biology Brussels and Molecular and Cellular Interactions, VIB, Brussels, Belgium, 2 Laboratoire de Chimie Generale, Institut de Pharmacie, Universite Libre de Bruxelles, Brussels, Belgium, 3 Interdisciplinary Research Institute, USR 3078 CNRS, Villeneuve d’Ascq, France Abstract Background: Chitin is a polysaccharide that forms the hard, outer shell of arthropods and the cell walls of fungi and some algae. Peptidoglycan is a polymer of sugars and amino acids constituting the cell walls of most bacteria. Enzymes that are able to hydrolyze these cell membrane polymers generally play important roles for protecting plants and animals against infection with insects and pathogens. A particular group of such glycoside hydrolase enzymes share some common features in their three-dimensional structure and in their molecular mechanism, forming the lysozyme superfamily. Results: Besides having a similar fold, all known catalytic domains of glycoside hydrolase proteins of lysozyme superfamily (families and subfamilies GH19, GH22, GH23, GH24 and GH46) share in common two structural elements: the central helix of the all-a domain, which invariably contains the catalytic glutamate residue acting as general-acid catalyst, and a b-hairpin pointed towards the substrate binding cleft. The invariant b-hairpin structure is intere