1E0G の概要
| エントリーDOI | 10.2210/pdb1e0g/pdb |
| 分子名称 | Membrane-bound lytic murein transglycosylase D (1 entity in total) |
| 機能のキーワード | cell wall, hydrolase, glycosidase, lipoprotein, outer membrane, multigene family |
| 由来する生物種 | Escherichia coli |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 5442.22 |
| 構造登録者 | |
| 主引用文献 | Bateman, A.,Bycroft, M. The Structure of a Lysm Domain from E.Coli Membrane Bound Lytic Murein Transglycosylase D (Mltd) J.Mol.Biol., 299:1113-, 2000 Cited by PubMed Abstract: The LysM domain is a widespread protein module. It was originally identified in enzymes that degrade bacterial cell walls but is also present in many other bacterial proteins. Several proteins that contain the domain, such as Staphylococcal IgG binding proteins and Escherichia coli intimin, are involved in bacterial pathogenesis. LysM domains are also found in some eukaryotic proteins, apparently as a result of horizontal gene transfer from bacteria. The available evidence suggests that the LysM domain is a general peptidoglycan-binding module. We have determined the structure of this domain from E. coli membrane-bound lytic murein transglycosylase D. The LysM domain has a betaalphaalphabeta secondary structure with the two helices packing onto the same side of an anti- parallel beta sheet. The structure shows no similarity to other bacterial cell surface domains. A potential binding site in a shallow groove on surface of the protein has been identified. PubMed: 10843862DOI: 10.1006/JMBI.2000.3778 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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