1QUS

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

Summary for 1QUS

• Entry DOI: 10.2210/pdb1qus/pdb
• Related: 1LTM
• Descriptor: LYTIC MUREIN TRANSGLYCOSYLASE B, SODIUM ION, BICINE, ... (5 entities in total)
• Functional Keywords: alpha-helical protein with an five-stranded antiparallel beta-sheet, hydrolase
• Biological source: Escherichia coli
• Cellular location: Cell outer membrane; Lipid-anchor; Periplasmic side: P41052
• Total number of polymer chains: 1
• Total formula weight: 36327.89

Authors

van Asselt, E.J.,Dijkstra, A.J.,Kalk, K.H.,Takacs, B.,Keck, W.,Dijkstra, B.W. (deposition date: 1999-07-03, release date: 1999-09-15, Last modification date: 2024-02-14)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.7 Å)