1QUS

1.7 A RESOLUTION STRUCTURE OF THE SOLUBLE LYTIC TRANSGLYCOSYLASE SLT35 FROM ESCHERICHIA COLI

1QUS の概要

• エントリーDOI: 10.2210/pdb1qus/pdb
• 関連するPDBエントリー: 1LTM
• 分子名称: LYTIC MUREIN TRANSGLYCOSYLASE B, SODIUM ION, BICINE, ... (5 entities in total)
• 機能のキーワード: alpha-helical protein with an five-stranded antiparallel beta-sheet, hydrolase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell outer membrane; Lipid-anchor; Periplasmic side: P41052
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36327.89

構造登録者

van Asselt, E.J.,Dijkstra, A.J.,Kalk, K.H.,Takacs, B.,Keck, W.,Dijkstra, B.W. (登録日: 1999-07-03, 公開日: 1999-09-15, 最終更新日: 2024-02-14)

主引用文献

van Asselt, E.J.,Dijkstra, A.J.,Kalk, K.H.,Takacs, B.,Keck, W.,Dijkstra, B.W.
Crystal structure of Escherichia coli lytic transglycosylase Slt35 reveals a lysozyme-like catalytic domain with an EF-hand.
Structure Fold.Des., 7:1167-1180, 1999

PubMed Abstract: Lytic transglycosylases are bacterial muramidases that catalyse the cleavage of the beta- 1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) in peptidoglycan with concomitant formation of a 1,6-anhydrobond in the MurNAc residue. These muramidases play an important role in the metabolism of the bacterial cell wall and might therefore be potential targets for the rational design of antibacterial drugs. One of the lytic transglycosylases is Slt35, a naturally occurring soluble fragment of the outer membrane bound lytic transglycosylase B (MltB) from Escherichia coli.

PubMed: 10545329
DOI: 10.1016/S0969-2126(00)80051-9

実験手法

X-RAY DIFFRACTION (1.7 Å)